Total chemical synthesis of the enzyme sortase A(DN59) with full catalytic activity - Deng, F. K.; Zhang, L.; Wang, Y. T.; Schneewind, O.; Kent, S. B. H. (Angew. Chem. Int. Ed., 2014)
The enzyme sortase A is a ligase which catalyzes transpeptidation reactions.1, 2 Surface proteins, including virulence factors, that have a C terminal recognition sequence are attached to Gly5 on the peptidoglycan of bacterial cell walls by sortase A.1 The enzyme is an important anti-virulence and anti-infective drug target for resistant strains of Gram-positive bacteria.2 In addition, because sortase A enables the splicing of polypeptide chains, the transpeptidation reaction catalyzed by sortase A is a potentially valuable tool for protein science.3 Here we describe the total chemical synthesis of enzymatically active sortase A. The target 148 residue polypeptide chain of sortase ADeltaN59 was synthesized by the convergent chemical ligation of four unprotected synthetic peptide segments. The folded protein molecule was isolated by size-exclusion chromatography and had full enzymatic activity in a transpeptidation assay. Total synthesis of sortase A will enable more sophisticated engineering of this important enzyme molecule.
AI038897/AI/NIAID NIH HHS/United States Journal Article Research Support, N.I.H., Extramural Germany
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, The University of Chicago, 929 East 57th Street, Chicago, IL 60637 (USA). alt-title: Angewandte Chemie (International ed number: 18 accession-num: 24668498
Keywords: Amino Acid Sequence; Catalysis; Molecular Sequence Data; Protein Folding; Aminoacyltransferases/*chemical synthesis/*metabolism; Bacterial Proteins/*chemical synthesis/*metabolism; Chromatography, Gel; Cysteine Endopeptidases/*chemical synthesis/*metabolism; Peptide Fragments/*chemistry/*metabolism; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Thiyl radicals in organic synthesis - Dénès, Fabrice; Pichowicz, Mark; Povie, Guillaume; Renaud, Philippe (Chem. Rev., 2014)
doi: 10.1021/cr400441m 0009-2665 doi: 10.1021/cr400441m
The following values have no corresponding Zotero field: number: 5 publisher: American Chemical Society

Chemical synthesis of the ATAD2 bromodomain - Creech, G. S.; Paresi, C.; Li, Y. M.; Danishefsky, S. J. (Proc. Natl. Acad. Sci. U. S. A., 2014)
Due to the emerging importance of the bromodomain binding region in the study of epigenetic effectors and the vast implications for a wide variety of human disease, the bromodomain region of human ATPase family AAA+ (ATPases associated with diverse cellular activities) domain-containing protein 2 (ATAD2) was targeted for chemical synthesis. The ATAD2 bromodomain (130 aa) was divided into five strategic fragments to be assembled using native chemical ligation with a focus on maximal convergency and efficiency. The fragments were assembled with one cysteine and three thioleucine ligations, unveiling the native alanine and leucine amino acids at the ligation points following metal-free dethiylation. Synthetic highlights of the study are a photolabile dimethoxynitrobenzyl-protected glutamic acid side chain used to impede hydrolysis of the C-terminal Glu-thioester, a thiazolidine-protected thioleucine, and an efficient assembly of three fragments in a single reaction vessel with dual-mode kinetic-standard chemical ligation. With a focus on material throughput and convergency, the five peptide fragments were assembled into the native ATAD2 bromodomain region with a total of three HPLC events in 8% overall yield from the fragments.
T32 GM073546/GM/NIGMS NIH HHS/United States F32 GM101746/GM/NIGMS NIH HHS/United States 5T32GM073546-07/GM/NIGMS NIH HHS/United States R01 GM102872/GM/NIGMS NIH HHS/United States GM102872-34/GM/NIGMS NIH HHS/United States Journal Article Research Support, N.I.H., Extramural United States
The following values have no corresponding Zotero field: auth-address: Bioorganic Chemistry Laboratory, Molecular Pharmacology and Chemistry Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065. alt-title: Proceedings of the National Academy of Sciences of the United States of America number: 8 accession-num: 24516155
Keywords: Humans; Solid-Phase Synthesis Techniques/*methods; Chromatography, High Pressure Liquid; Mass Spectrometry; *Protein Structure, Tertiary; Adenosine Triphosphatases/*chemical synthesis; DNA-Binding Proteins/*chemical synthesis; Magnetic Resonance Spectroscopy; Peptide Fragments/*chemistry

Activities at the universal protein resource (UniProt) - UniProt Consortium (Nucleic Acids Res., 2014)
The following values have no corresponding Zotero field: alt-title: Nucleic acids research number: Database issue accession-num: 24253303
Keywords: *Databases, Protein; *Sequence Analysis, Protein; Gene Ontology; Genomics; Internet; Molecular Sequence Annotation; Proteins/genetics; Proteomics

Decoration of silicon nanostructures with copper particles for simultaneous selective capture and mass spectrometry detection of His-tagged model peptide - Coffinier, Y.; Kurylo, I.; Drobecq, H.; Szunerits, S.; Melnyk, O.; Zaitsev, V. N.; Boukherroub, R. (Analyst, 2014)
We present in this work a simple and fast preparation method of a new affinity surface-assisted laser/desorption ionization mass spectrometry (SALDI-MS) substrate based on silicon nanostructures decorated with copper particles. The silicon nanostructures were fabricated by the metal-assisted chemical etching (MACE) method. Then, superhydrophilic areas surrounded by superhydrophobic regions were formed through hydrosilylation reaction of 1-octadecene, followed by local degradation of the octadecyl layer. After that, copper particles were deposited in the hydrophilic areas by using the electroless method. We have demonstrated that these surfaces were able to perform high selective capture of model His-tag peptide even in a complex mixture such as serum solution. Then, the captured peptide was detected by mass spectrometry at a femtomolar level without the need of organic matrix.
Cited By :4
Cited By :4
Coffinier, Yannick Kurylo, Ievgen Drobecq, Herve Szunerits, Sabine Melnyk, Oleg Zaitsev, Vladimir N Boukherroub, Rabah England The Analyst Analyst. 2014 Oct 21;139(20):5155-63. doi: 10.1039/c4an01056f. Epub 2014 Aug 12.
Export Date: 25 May 2018
Export Date: 25 May 2018

One-pot peptide ligation-desulfurization at glutamate - Cergol, Katie M.; Thompson, Robert E.; Malins, Lara R.; Turner, Peter; Payne, Richard J. (Org. Lett., 2014)
doi: 10.1021/ol403288n 1523-7060 doi: 10.1021/ol403288n
The following values have no corresponding Zotero field: number: 1 publisher: American Chemical Society

Cyclic-disulfide-based prodrugs for cytosol-specific drug delivery - Butora, Gabor; Qi, Ning; Fu, Wenlang; Nguyen, Truyen; Huang, Hsueh-Cheng; Davies, Ian W. (Angew. Chem. Int. Ed., 2014)
The cytosolic conversion of therapeutically relevant nucleosides into bioactive triphosphates is often hampered by the inefficiency of the first kinase-mediated step. Nucleoside monophosphate prodrugs can be used to bypass this limitation. Herein we describe a novel cyclic-disulfide class of nucleoside monophosphate prodrugs with a cytosol-specific, reductive release trigger. The key event, a charge-dissipating reduction-triggered cyclodeesterification leads to robust cytosolic production of the cyclic 3′,5′-monophosphate for downstream enzymatic processing. The antiviral competence of the platform was demonstrated with an O-benzyl-1,2-dithiane-4,5-diol ester of 2′-C-methyluridine-3′,5′-phosphate. Both in vitro and in vivo comparison with the clinically efficacious ProTide prodrug of 2′-deoxy-2′-α-fluoro-β-C-methyluridine is provided. The cytosolic specificity of the release allows for a wide range of potential applications, from tissue-targeted drug delivery to intracellular imaging.
1521-3773
The following values have no corresponding Zotero field: number: 51 publisher: WILEY-VCH Verlag
Keywords: antiviral agents; drug delivery; kinase bypass; nucleosides; prodrugs

In situ thioester formation for protein ligation using a-methylcysteine - Burlina, Fabienne; Papageorgiou, George; Morris, Caroline; White, Peter D.; Offer, John (Chem. Sci., 2014)
The progress of total chemical protein synthesis has been hampered by difficulties in preparing peptide thioesters by standard Fmoc peptide synthesis. The amino acid, [small alpha]-methylcysteine, sited at the C-terminus of a peptide can substitute for a thioester in peptide ligation reactions. C-terminal [small alpha]-methylcysteine is fully compatible with Fmoc peptide synthesis and its use in ligation is very simple and robust. Its potential is demonstrated with the synthesis of model proteins.
10.1039/C3SC52140K
The following values have no corresponding Zotero field: number: 2 publisher: The Royal Society of Chemistry

High-throughput synthesis of peptide alpha-thioesters: a safety catch linker approach enabling parallel hydrogen fluoride cleavage - Brust, A.; Schroeder, C. I.; Alewood, P. F. (ChemMedChem, 2014)
Peptide alpha-thioesters are fundamental building blocks in peptide and protein science, providing powerful tools for peptide medicinal chemistry. The application of peptide alpha-thioesters in native chemical ligation reactions has enabled synthetic access to cysteine-rich peptides and proteins, cyclic peptides as well as labeled and chemically modified biomolecules. An efficient high-throughput synthesis of peptide alpha-thioester building blocks would be beneficial for many medicinal chemical applications that require peptides and proteins. Herein we present a novel synthetic route to cysteine-rich peptide alpha-thioesters using a safety catch linker that enables a parallel synthetic strategy for chemical protein synthesis. ACP(68-75), bradykinin and dynorphin(1-13) were synthesized via Boc chemistry in their thioester form on a safety catch amide linker (SCAL), employing polystyrene- or poly(ethylene glycol)-based resins, compartmentalized in tea bags. This compartmentalized resin/linker strategy facilitated a parallel hydrogen fluoride cleavage in which each peptide thioester was subsequently cyclized by native chemical ligation, demonstrating the utility of this approach. A naturally occurring bioactive cyclic peptide, the sunflower trypsin inhibitor SFTI-1, was synthesized to demonstrate the viability of this method to access important peptide biomolecules.
Brust, Andreas Schroeder, Christina I Alewood, Paul F Germany ChemMedChem. 2014 May;9(5):1038-46. doi: 10.1002/cmdc.201300524. Epub 2014 Mar 3.
The following values have no corresponding Zotero field: auth-address: Institute of Molecular Bioscience, The University of Queensland, Brisbane, 4072 (Australia). a.brust@imb.uq.edu.au. alt-title: ChemMedChem number: 5 edition: 2014/03/05 accession-num: 24591329 work-type: Research Support, Non-U.S. Gov't
Keywords: Molecular Structure; Cyclization; Esters/*chemical synthesis/*chemistry; Hydrofluoric Acid/*chemistry; Peptides/*chemical synthesis/*chemistry; Sulfhydryl Compounds/*chemical synthesis/*chemistry

A novel PEG-based solid support enables the synthesis of >50 amino-acid peptide thioesters and the total synthesis of a functional SUMO-1 peptide conjugate - Boll, E.; Drobecq, H.; Ollivier, N.; Raibaut, L.; Desmet, R.; Vicogne, J.; Melnyk, O. (Chem. Sci., 2014)
A bis(2-sulfanylethyl)amino PEG-based resin enabled the synthesis of large ([similar]50 Aa) SEA or thioester peptides using Fmoc-SPPS. These peptide segments permitted the first total synthesis of a 97 amino-acid long SUMO-1-SEA peptide thioester surrogate and of a functional and reversible SUMO-1 peptide conjugate.
10.1039/C3SC53509F
Cited By :16
Cited By :16
Cited By :16
Export Date: 25 May 2018

Thiocarbamate-linked polysulfonate-peptide conjugates as selective hepatocyte growth factor receptor binders - Besret, S.; Vicogne, J.; Dahmani, F.; Fafeur, V.; Desmet, R.; Drobecq, H.; Romieu, A.; Melnyk, P.; Melnyk, O. (Bioconjugate Chem., 2014)
The capacity of many proteins to interact with natural or synthetic polyanions has been exploited for modulating their biological action. However, the polydispersity of these macromolecular polyanions as well as their poor specificity is a severe limitation to their use as drugs. An emerging trend in this field is the synthesis of homogeneous and well-defined polyanion-peptide conjugates, which act as bivalent ligands, with the peptide part bringing the selectivity of the scaffold. Alternately, this strategy can be used for improving the binding of short peptides to polyanion-binding protein targets. This work describes the design and first synthesis of homogeneous polysulfonate-peptide conjugates using thiocarbamate ligation for binding to the extracellular domain of MET tyrosine kinase receptor for hepatocyte growth factor.
Besret, Soizic Vicogne, Jerome Dahmani, Fatima Fafeur, Veronique Desmet, Remi Drobecq, Herve Romieu, Anthony Melnyk, Patricia Melnyk, Oleg Research Support, Non-U.S. Gov't United States Bioconjugate chemistry Bioconjug Chem. 2014 May 21;25(5):1000-10. doi: 10.1021/bc500137j. Epub 2014 May 5.
Cited By :1
Cited By :1
Cited By :1
Export Date: 25 May 2018

Peptidomimetics via modifications of amino acids and peptide bonds - Avan, Ilker; Hall, C. Dennis; Katritzky, Alan R. (Chem. Soc. Rev., 2014)
Peptidomimetics represent an important field in chemistry, pharmacology and material science as they circumvent the limitations of traditional peptides used in therapy. Self-structural organizations such as turns, helices, sheets and loops can be accessed by chemical modifications of amino acids or peptides. In-depth structural and conformational analysis and structure-activity relationships (SAR) offer a way to establish peptidomimetic libraries. Herein, we review recent developments in peptidomimetics that are formed via heteroatom replacement within the native amino acid backbone. Each sub-section describes structural features, utility and preparative methods.
The following values have no corresponding Zotero field: number: 10 publisher: The Royal Society of Chemistry work-type: 10.1039/C3CS60384A

Chemical synthesis of proteins using peptide hydrazides as thioester surrogates - Zheng, J.-S.; Tang, S.; Qi, Y.-K.; Wang, Z.-P.; Liu, L. (Nat. Protocols, 2013)
This protocol provides a detailed procedure for the chemical synthesis of proteins through native chemical ligation of peptide hydrazides. The two crucial stages of this protocol are (i) the solid-phase synthesis of peptide hydrazides via Fmoc chemistry and (ii) the native chemical ligation of peptide hydrazides through in situNaNO2 activation and thiolysis. This protocol may be of help in the synthesis of proteins that are not easily produced by recombinant technology and that include acid-sensitive modifications; it also does not involve the use of hazardous HF. The utility of the protocol is shown for the total synthesis of 140-aa-long Î±-synuclein, a protein that has an important role in the development of Parkinson's disease. The whole synthesis of the target protein Î±-synuclein in milligram scale takes âˆ¼30 working days.
Protocol
The following values have no corresponding Zotero field: number: 12 publisher: Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.

Development of new thioester equivalents for protein chemical synthesis - Zheng, J.-S.; Tang, S.; Huang, Y.-C.; Liu, L. (Acc. Chem. Res., 2013)
The chemical synthesis of proteins provides synthetic chemists with an interesting challenge and supports biological research through the generation of proteins that are not produced naturally. Although it offers advantages, studies of solid phase peptide synthesis have established limits for this technique: researchers can only prepare peptides up to 50 amino acids in length in sufficient yields and purity. Therefore, researchers have developed techniques to condense peptide segments to build longer polypeptide chains. The method of choice for chemical synthesis of these longer polypeptides is convergent condensation of unprotected protein fragments by the native chemical ligation reaction in aqueous buffer. As researchers apply this strategy to increasingly difficult protein targets, they have needed to overcome diverse problems such as the requirement for a thiol-containing amino acid residue at the ligation site, the difficulty in synthesizing thioester intermediates under mild conditions, and the challenge of condensing multiple peptide segments with higher efficiency. In this Account, we describe our research toward the development of new thioester equivalents for protein chemical synthesis. We have focused on a simple idea of finding new chemistry to selectively convert a relatively ?low-energy? acyl group such as an ester or amide to a thioester under mild conditions. We have learned that this seemingly unfavorable acyl substitution process can occur by the coupling of the ester or amide with another energetically favorable reaction, such as the irreversible hydrolysis of an enamine or condensation of a hydrazide with nitrous acid. Using this strategy, we have developed several new thioester equivalents that we can use for the condensation of protein segments. These new thioester equivalents not only improve the efficiency for the preparation of the intermediates needed for protein chemical synthesis but also allow for the design of new convergent routes for the condensation of multiple protein fragments.
doi: 10.1021/ar400012w
The following values have no corresponding Zotero field: publisher: American Chemical Society

Protein chemical synthesis by serine and threonine ligation - Zhang, Y.; Xu, C.; Lam, H. Y.; Lee, C. L.; Li, X. (Proc. Natl. Acad. Sci. U. S. A., 2013)
An efficient method has been developed for the salicylaldehyde ester-mediated ligation of unprotected peptides at serine (Ser) or threonine (Thr) residues. The utility of this peptide ligation approach has been demonstrated through the convergent syntheses of two therapeutic peptides--ovine-corticoliberin and Forteo--and the human erythrocyte acylphosphatase protein ( approximately 11 kDa). The requisite peptide salicylaldehyde ester precursor is prepared in an epimerization-free manner via Fmoc-solid-phase peptide synthesis.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, The University of Hong Kong, Hong Kong, People's Republic of China. number: 17 edition: 2013/04/10 accession-num: 23569249
Zhang, Yinfeng Xu, Ci Lam, Hiu Yung Lee, Chi Lung Li, Xuechen Research Support, Non-U.S. Gov't United States Proceedings of the National Academy of Sciences of the United States of America Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):6657-62. doi: 10.1073/pnas.1221012110. Epub 2013 Apr 8.
Keywords: Animals; Humans; Peptides/*chemistry; Molecular Structure; Chromatography, High Pressure Liquid; Mass Spectrometry; Protein Engineering/*methods; Acid Anhydride Hydrolases/*chemical synthesis; Aldehydes/*chemistry; Corticotropin-Releasing Hormone/*chemical synthesis; Serine/chemistry; Sheep; Teriparatide/*chemical synthesis; Threonine/chemistry

Chemical synthesis of a masked analogue of the fish antifreeze potentiating protein (AFPP) - Yang, Sung-Hyun; Wojnar, Joanna M.; Harris, Paul W. R.; DeVries, Arthur L.; Evans, Clive W.; Brimble, Margaret A. (Org. Biomol. Chem., 2013)
A recently identified Antarctic fish protein termed antifreeze potentiating protein (AFPP) is thought to act as an adjunct to the previously characterised antifreeze glycoproteins (AFGPs), the two acting together to inhibit ice crystal growth in vivo. Elucidating the functional properties of the new AFPP requires access to large amounts of pure product, but the paucity of natural material necessitates alternative approaches. We therefore embarked on the total chemical synthesis of the AFPP, through a convergent ligation strategy. After many challenges, mostly due to the solubility issues of the peptide fragments, and several revisions of the original synthetic strategy, we have successfully synthesized a masked analogue of AFPP. The key to the successful synthesis was the use of a solubilising tag attached through a hydrolysable linker.
The following values have no corresponding Zotero field: number: 30 publisher: The Royal Society of Chemistry work-type: 10.1039/C3OB41066H

Convergent synthesis of MUC1 glycopeptides via serine ligation - Xu, C.; Lam, H. Y.; Zhang, Y.; Li, X. (Chem. Commun., 2013)
Syntheses of MUC1 glycopeptides (40-mer and 80-mer) are described. The convergent synthesis was achieved by native serine ligation using side-chain unprotected glycopeptide segments.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, The University of Hong Kong, Hong Kong, P. R. China. xuechenl@hku.hk. number: 55 edition: 2013/06/05 accession-num: 23732560
Xu, Ci Lam, Hiu Yung Zhang, Yinfeng Li, Xuechen England Chemical communications (Cambridge, England) Chem Commun (Camb). 2013 Jun 13;49(55):6200-2. doi: 10.1039/c3cc42573h.

Orthogonality in organic, polymer, and supramolecular chemistry: from Merrifield to click chemistry - Wong, Chun-Ho; Zimmerman, Steven C. (Chem. Commun., 2013)
The concept of orthogonality has been applied to many areas of chemistry, ranging from wave functions to chromatography. But it was Barany and Merrifield's orthogonal protecting group strategy that paved the way for solid phase peptide syntheses, other important classes of biomaterials such as oligosaccharides and oligonucleotides, and ultimately to a term in widespread usage that is focused on chemical reactivity and binding selectivity. The orthogonal protection strategy has been extended to the development of orthogonal activation, and recently the click reaction, for streamlining organic synthesis. The click reaction and its variants are considered orthogonal as the components react together in high yield and in the presence of many other functional groups. Likewise, supramolecular building blocks can also be orthogonal, thereby enabling programmed self-assembly, a superb strategy to create complex architectures. Overall, orthogonal reactions and supramolecular interactions have dramatically improved the syntheses, the preparation of functional materials, and the self-assembly of nanoscale structures.
10.1039/C2CC37316E
The following values have no corresponding Zotero field: number: 17 publisher: The Royal Society of Chemistry

Reconstitution of the catalytic core of F-ATPase (ab)3g from Escherichia coli using chemically synthesized subunit g - Wintermann, F.; Engelbrecht, S. (Angew. Chem. Int. Ed., 2013)
The following values have no corresponding Zotero field: auth-address: Universitat Osnabruck, Fachbereich Biologie/Chemie, Abt. Biochemie, Barbarastrasse 13, 49076 Osnabruck, Germany. frank.wintermann@biologie.uni-osnabrueck.de number: 4 edition: 2012/12/06 accession-num: 23212931
Wintermann, Frank Engelbrecht, Siegfried Research Support, Non-U.S. Gov't Germany Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2013 Jan 21;52(4):1309-13. doi: 10.1002/anie.201206744. Epub 2012 Dec 4.

Solid-phase peptide synthesis and solid-phase fragment coupling mediated by isonitriles - Wang, T.; Danishefsky, S. J. (Proc Natl Acad Sci U S A, 2013)
The synthesis of polypeptides on solid phase via mediation by isonitriles is described. The acyl donor is a thioacid, which presumably reacts with the isonitrile to generate a thio-formimidate carboxylate mixed anhydride intermediate. Applications of this chemistry to reiterative solid-phase peptide synthesis as well as solid-phase fragment coupling are described.
The following values have no corresponding Zotero field: auth-address: Laboratory of Bioorganic Chemistry, Memorial Sloan-Kettering Cancer Center, New York, NY 10065. number: 29 edition: 2013/07/04 accession-num: 23821753
Wang, Ting Danishefsky, Samuel J United States Proceedings of the National Academy of Sciences of the United States of America Proc Natl Acad Sci U S A. 2013 Jul 16;110(29):11708-13. doi: 10.1073/pnas.1310431110. Epub 2013 Jul 2.

Site-specific peptide and protein immobilization on surface plasmon resonance chips via strain-promoted cycloaddition - Wammes, A. E.; Fischer, M. J.; de Mol, N. J.; van Eldijk, M. B.; Rutjes, F. P.; van Hest, J. C.; van Delft, F. L. (Lab. Chip., 2013)
Surface plasmon resonance (SPR) is a powerful label-free diagnostic tool to study biomolecular interactions. However, one of the drawbacks of SPR is the lack of controlled immobilization of ligands on the sensor surface. We have developed a modular platform for the fast, reagent-free and site-specific immobilization of azide-containing ligands by strain-promoted cycloaddition onto a cyclooctyne-modified SPR sensor surface. The usefulness of the concept was shown in a study with a papain model system, and up to 150 experiments were performed without loss of surface quality. Furthermore, azide-containing green fluorescent protein (GFP) was also effectively immobilized. Taken together, cyclooctyne-modified SPR chips enable smooth and site-selective immobilization of ligands and prove to be more robust than traditionally functionalized systems.
The following values have no corresponding Zotero field: auth-address: Radboud University, Institute for Molecules and Materials, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands. f.vandelft@science.ru.nl. number: 10 edition: 2013/04/05 accession-num: 23552823
Wammes, Angelique E M Fischer, Marcel J E de Mol, Nico J van Eldijk, Mark B Rutjes, Floris P J T van Hest, Jan C M van Delft, Floris L England Lab on a chip Lab Chip. 2013 Apr 23;13(10):1863-7. doi: 10.1039/c3lc41338a. Epub 2013 Apr 4.

Expanding chemical diversity of conotoxins: peptoid-peptide chimeras of the sodium channel blocker mu-KIIIA and its selenopeptide analogues - Walewska, A.; Han, T. S.; Zhang, M. M.; Yoshikami, D.; Bulaj, G.; Rolka, K. (Eur J Med Chem, 2013)
The mu-conotoxin KIIIA is a three disulfide-bridged blocker of voltage-gated sodium channels (VGSCs). The Lys(7) residue in KIIIA is an attractive target for manipulating the selectivity and efficacy of this peptide. Here, we report the design and chemical synthesis of mu-conopeptoid analogues (peptomers) in which we replaced Lys(7) with peptoid monomers of increasing side-chain size: N-methylglycine, N-butylglycine and N-octylglycine. In the first series of analogues, the peptide core contained all three disulfide bridges; whereas in the second series, a disulfide-depleted selenoconopeptide core was used to simplify oxidative folding. The analogues were tested for functional activity in blocking the Nav1.2 subtype of mammalian VGSCs exogenously expressed in Xenopus oocytes. All six analogues were active, with the N-methylglycine analogue, [Sar(7)]KIIIA, the most potent in blocking the channels while favouring lower efficacy. Our findings demonstrate that the use of N-substituted Gly residues in conotoxins show promise as a tool to optimize their pharmacological properties as potential analgesic drug leads.
P01 GM048677/GM/NIGMS NIH HHS/United States P01 GM48677/GM/NIGMS NIH HHS/United States Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't France
The following values have no corresponding Zotero field: auth-address: Faculty of Chemistry, University of Gdansk, Sobieskiego 18, 80-952 Gdansk, Poland. walewska@chem.univ.gda.pl alt-title: European journal of medicinal chemistry accession-num: 23707919
Keywords: Peptides/*chemistry; Molecular Structure; Conotoxins/*chemistry; Peptoids/*chemistry; Selenoproteins/chemical synthesis/chemistry/*pharmacology; Structure-Activity Relationship; Voltage-Gated Sodium Channel Blockers/chemical synthesis/chemistry/*pharmacology; Voltage-Gated Sodium Channels/*metabolism

Recent progress in intein research: from mechanism to directed evolution and applications - Volkmann, G.; Mootz, H. D. (Cell Mol Life Sci, 2013)
Inteins catalyze a post-translational modification known as protein splicing, where the intein removes itself from a precursor protein and concomitantly ligates the flanking protein sequences with a peptide bond. Over the past two decades, inteins have risen from a peculiarity to a rich source of applications in biotechnology, biomedicine, and protein chemistry. In this review, we focus on developments of intein-related research spanning the last 5 years, including the three different splicing mechanisms and their molecular underpinnings, the directed evolution of inteins towards improved splicing in exogenous protein contexts, as well as novel applications of inteins for cell biology and protein engineering, which were made possible by a clearer understanding of the protein splicing mechanism.
The following values have no corresponding Zotero field: auth-address: Institute of Biochemistry, University of Munster, Wilhelm-Klemm-Str. 2, 48149, Munster, Germany. number: 7 edition: 2012/08/29 accession-num: 22926412
Volkmann, Gerrit Mootz, Henning D Research Support, Non-U.S. Gov't Review Switzerland Cellular and molecular life sciences : CMLS Cell Mol Life Sci. 2013 Apr;70(7):1185-206. doi: 10.1007/s00018-012-1120-4. Epub 2012 Aug 28.
Keywords: Animals; Humans; Biomedical Research/methods/*trends; Biotechnology/methods/trends; Directed Molecular Evolution/*methods/trends; Inteins/genetics/*physiology; Models, Biological; Protein Engineering/methods/*trends; Protein Processing, Post-Translational/genetics/physiology; Protein Splicing/genetics/physiology

SUMOylated RanGAP1 prepared by click chemistry - Van Treel, N. D.; Mootz, H. D. (J. Pept. Sci., 2013)
Ubiquitin and ubiquitin-like proteins such as SUMO represent important and abundant post-translational modifications involved in many cellular processes. These modifiers are reversibly attached via an isopeptide bond to lysine side chains of their target proteins by the action of specific E1, E2, and E3 enzymes. A significant challenge in studying ubiquitylation and SUMOylation is the frequently encountered inability to access desired conjugates at a defined position of the target protein and in homogenous form by using enzymatic preparation. In recent years, several chemical conjugation approaches have been developed to overcome this limitation. In this study, we aimed to selectively SUMOylate a 189-amino acid fragment of human RanGAP1 (amino acids 398-587) at the position of Lys524 by applying two recently reported approaches based on the Cu(I)-catalyzed alkyne-azide cycloaddition. Because of low yields observed for the incorporation of an unnatural amino acid with an azide moiety by the tRNA suppression technology, this route was abandoned. However, installing a single cysteine at position 524 and its selective alkylation was successful to introduce the azide group. The triazole-linked SUMO1**RanGAP1 conjugate could be obtained in good yields, purified, and was shown to specifically interact with RanBP2/Ubc9. Thus, we expand the scope of proteins accessible to chemical conjugation with ubiquitin-like proteins and underline the importance of having alternative approaches to do so. Copyright (c) 2013 European Peptide Society and John Wiley & Sons, Ltd.
Journal Article Research Support, Non-U.S. Gov't England an official publication of the European Peptide Society
The following values have no corresponding Zotero field: auth-address: Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Str. 2, 48149, Munster, Germany. number: 2 edition: 2013/12/18 accession-num: 24338848
The following values have no corresponding Zotero field: auth-address: Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Str. 2, 48149, Munster, Germany. Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Str. 2, 48149, Munster, Germany. number: 2 accession-num: 24338848
van Treel, Nadine D Mootz, Henning D Journal article Journal of peptide science : an official publication of the European Peptide Society J Pept Sci. 2013 Dec 15. doi: 10.1002/psc.2591.
Keywords: Models, Molecular; Catalysis; Copper/chemistry; Protein Processing, Post-Translational; *Click Chemistry; GTPase-Activating Proteins/*chemical synthesis/chemistry; Sumoylation

Chemical assembly of N-glycoproteins: a refined toolbox to address a ubiquitous posttranslational modification - Unverzagt, C.; Kajihara, Y. (Chem. Soc. Rev., 2013)
Incremental developments in the chemistry of peptides, proteins and carbohydrates have enabled researchers to assemble entire glycoproteins with high precision. Based on sophisticated ligation chemistries pure glycoproteins bearing a single glycosylation pattern have become available. The impact of N-glycosylation on the function of glycoproteins is generally recognized but not well understood. Based on the recent advances in the synthesis of glycoproteins by chemical methods researchers can finally start to elucidate the various roles of carbohydrates in complex biomolecules in detail.
The following values have no corresponding Zotero field: auth-address: Bioorganische Chemie, Gebaude NWI, Universitat Bayreuth, 95440 Bayreuth, Germany. carlo.unverzagt@uni-bayreuth.de number: 10 edition: 2013/02/14 accession-num: 23403448
Unverzagt, Carlo Kajihara, Yasuhiro England Chemical Society reviews Chem Soc Rev. 2013 May 21;42(10):4408-20. doi: 10.1039/c3cs35485g. Epub 2013 Feb 13.

Enzyme-labile protecting groups for the synthesis of natural products: solid-phase synthesis of thiocoraline - Tulla-Puche, J.; Gongora-Benitez, M.; Bayo-Puxan, N.; Francesch, A. M.; Cuevas, C.; Albericio, F. (Angew. Chem. Int. Ed., 2013)
The following values have no corresponding Zotero field: auth-address: Institute for Research in Biomedicine Barcelona, CIBER-BBN, Baldiri Reixac 10, 08028 Barcelona, Spain. judit.tulla@irbbarcelona.org number: 22 edition: 2013/04/27 accession-num: 23619769 work-type: Research Support, Non-U.S. Gov't
Tulla-Puche, Judit Gongora-Benitez, Miriam Bayo-Puxan, Nuria Francesch, Andres M Cuevas, Carmen Albericio, Fernando Germany International ed. in English Angew Chem Int Ed Engl. 2013 May 27;52(22):5726-30. doi: 10.1002/anie.201301708. Epub 2013 Apr 25.
Keywords: Molecular Structure; Chromatography, High Pressure Liquid; *Solid-Phase Synthesis Techniques; Biological Products/*chemical synthesis; Depsipeptides/*chemical synthesis; Staining and Labeling

Chemoselective peptide ligation-desulfurization at aspartate - Thompson, R. E.; Chan, B.; Radom, L.; Jolliffe, K. A.; Payne, R. J. (Angew. Chem. Int. Ed., 2013)
Journal Article Research Support, Non-U.S. Gov't Germany
The following values have no corresponding Zotero field: auth-address: School of Chemistry, The University of Sydney, NSW 2006, Australia. alt-title: Angewandte Chemie (International ed number: 37 accession-num: 23893778
Keywords: Amino Acid Sequence; Peptides/chemical synthesis/*chemistry; Aspartic Acid/*chemistry; Sulfur/*chemistry

Expressed protein ligation at methionine: N-terminal attachment of homocysteine, ligation, and masking - Tanaka, T.; Wagner, A. M.; Warner, J. B.; Wang, Y. J.; Petersson, E. J. (Angew. Chem. Int. Ed., 2013)
S10 RR023444/RR/NCRR NIH HHS/United States RR-023444/RR/NCRR NIH HHS/United States Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Germany
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104-6323, USA. alt-title: Angewandte Chemie (International ed number: 24 accession-num: 23629972
Keywords: Proteins/*chemistry; Homocysteine/*chemistry; Methionine/*chemistry

A thioethylalkylamido (TEA) thioester surrogate in the synthesis of a cyclic peptide via a tandem acyl shift - Taichi, M.; Hemu, X.; Qiu, Y.; Tam, J. P. (Org. Lett., 2013)
The cyclic cystine-knot peptide, kalata B1, was synthesized by employing a novel Fmoc-compatible thioethylalkylamido (TEA) thioester surrogate via an N-S acyl shift followed by a thiol-thioester exchange reaction. TEA thioester surrogate is cost-effective, conveniently prepared in one-step with starting materials, readily available from commercial sources, and highly efficient in preparing peptide thioesters.
Taichi, Misako Hemu, Xinya Qiu, Yibo Tam, James P Research Support, Non-U.S. Gov't United States Organic letters Org Lett. 2013 Jun 7;15(11):2620-3. doi: 10.1021/ol400801k. Epub 2013 May 13.
The following values have no corresponding Zotero field: auth-address: School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551. number: 11 edition: 2013/05/15 accession-num: 23668312

Role of solvent on nonenzymatic peptide bond formation mechanisms and kinetic isotope effects - Swiderek, Katarzyna; Tunon, Inaki; Marti, Sergio; Moliner, Vicent; Bertran, Juan (J. Am. Chem. Soc., 2013)
doi: 10.1021/ja403038t 0002-7863 doi: 10.1021/ja403038t
The following values have no corresponding Zotero field: number: 23 publisher: American Chemical Society

Convergent chemical synthesis of histone H2B protein for the site-specific ubiquitination at Lys34 - Siman, P.; Karthikeyan, S. V.; Nikolov, M.; Fischle, W.; Brik, A. (Angew. Chem. Int. Ed., 2013)
Siman, Peter Karthikeyan, Subramanian Vedhanarayanan Nikolov, Miroslav Fischle, Wolfgang Brik, Ashraf Research Support, Non-U.S. Gov't Germany Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2013 Jul 29;52(31):8059-63. doi: 10.1002/anie.201303844. Epub 2013 Jun 21.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Ben Gurion University of the Negev, Beer Sheva 84105, Israel. number: 31 edition: 2013/06/25 accession-num: 23794525

Extein Residues Play an Intimate Role in the Rate-Limiting Step of Protein Trans-Splicing - Shah, Neel H.; Eryilmaz, Ertan; Cowburn, David; Muir, Tom W. (J. Am. Chem. Soc., 2014)
doi: 10.1021/ja401015p
The following values have no corresponding Zotero field: number: 15 publisher: American Chemical Society

Chemical synthesis of biologically active monoglycosylated GM2-activator protein analogue using N-sulfanylethylanilide peptide - Sato, K.; Shigenaga, A.; Kitakaze, K.; Sakamoto, K.; Tsuji, D.; Itoh, K.; Otaka, A. (Angew. Chem. Int. Ed., 2013)
Going to SEA(lide): Total chemical synthesis of a 162-residue glycoprotein analogue of the monoglycosylated human GM2-activator protein (GM2AP) was achieved. Key steps were the use of N-sulfanylethylanilide (SEAlide) peptides in the kinetic chemical ligation synthesis of a large peptide fragment, and a convergent native chemical ligation for final fragment assembly.
Sato, Kohei Shigenaga, Akira Kitakaze, Keisuke Sakamoto, Ken Tsuji, Daisuke Itoh, Kohji Otaka, Akira Journal article Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2013 Jun 13. doi: 10.1002/anie.201303390.
The following values have no corresponding Zotero field: auth-address: Institute of Health Bioscience and Graduate School of Pharmaceutical Sciences, The University of Tokushima, Shomachi, Tokushima 770-8505 (Japan). number: 30 edition: 2013/06/15 accession-num: 23765733

Bioorthogonal reactions challenged: DNA templated native chemical ligation during PCR - Roloff, Alexander; Seitz, Oliver (Chem. Sci., 2013)
DNA directed chemistry is commonly performed by using nanomolar amounts of DNA templates. Herein we introduce a method that allows the use of attomolar template loads. A DNA templated native chemical ligation yields to the covalent fixation of two fluorophores while the template is being produced during polymerase chain reaction.
10.1039/C2SC20961F
The following values have no corresponding Zotero field: number: 1 publisher: The Royal Society of Chemistry

A kinetic isotope effect and isotope exchange study of the nonenzymatic and the equine serum butyrylcholinesterase-catalyzed thioester hydrolysis - Robins, Lori I.; Meisenheimer, Kristen M.; Fogle, Emily J.; Chaplan, Cory A.; Redman, Richard L.; Vacca, Joseph T.; Tellier, Michelle R.; Collins, Brittney R.; Duong, Dorothea H.; Schulz, Kathrin; Marlier, John F. (J. Org. Chem., 2013)
doi: 10.1021/jo402063k 0022-3263 doi: 10.1021/jo402063k
The following values have no corresponding Zotero field: number: 23 publisher: American Chemical Society

Total synthesis of biotinylated N domain of human hepatocyte growth factor - Raibaut, L.; Vicogne, J.; Leclercq, B.; Drobecq, H.; Desmet, R.; Melnyk, O. (Bioorg. Med. Chem., 2013)
Hepatocyte growth factor/scatter factor (HGF/SF) is the high affinity ligand of MET tyrosine kinase receptor. We report here the total synthesis of a biotinylated analogue of human HGF/SF N domain. Functionally, N domain is part of the HGF/SF high affinity binding site for MET and also the main HGF/SF binding site for heparin. The 97 Aa linear chain featuring a C-terminal biotin group was assembled in high yield using an N-to-C one-pot three segments assembly strategy relying on a sequential Native Chemical Ligation (NCL)/bis(2-sulfanylethyl)amido (SEA) native peptide ligation process. The folded protein displayed the native disulfide bond pattern and showed the ability to bind heparin.
Cited By :11
Cited By :11
Cited By :11
Export Date: 25 May 2018
Export Date: 25 May 2018

Bis(2-sulfanylethyl)amido peptides enable native chemical ligation at proline and minimize deletion side-product formation - Raibaut, L.; Seeberger, P.; Melnyk, O. (Org. Lett., 2013)
Native chemical ligation of C-terminal peptidyl prolyl alkylthioesters with N-terminal cysteinyl peptides usually exhibits poor kinetic rates compared to other C-terminal amino acid residues. It is shown here that the reaction is accompanied by the formation of a deletion side product which is minimized by using a bis(2-sulfanylethyl)amido (SEA) thioester surrogate at a mildly acidic pH.
Cited By :20
Export Date: 25 May 2018
Raibaut, Laurent Seeberger, Phillip Melnyk, Oleg Journal article Organic letters Org Lett. 2013 Oct 11.
The following values have no corresponding Zotero field: auth-address: UMR CNRS 8161, Pasteur Institute of Lille , 59021 Lille, France. number: 21 edition: 2013/10/15 accession-num: 24117240

Highly efficient solid phase synthesis of large polypeptides by iterative ligations of bis(2-sulfanylethyl)amido (SEA) peptide segments - Raibaut, Laurent; Adihou, Helene; Desmet, Remi; Delmas, Agnes F.; Aucagne, Vincent; Melnyk, Oleg (Chem. Sci., 2013)
Up to now, the advantages of solid phase protein synthesis have been largely under-utilized due to the difficulty of designing a simple and efficient elongation cycle enabling the concatenation of unprotected peptide segments. The combination of selective N-terminal anchoring (N3-Esoc linker) with the blocked thioester properties of the SEAoff group enabled the solid phase concatenation of unprotected peptide segments by N-to-C sequential formation of native peptide bonds. The strategy was applied to the synthesis of a 60 amino acid-long latent peptide thioester or to the assembly of five peptide segments to give a 15 kDa polypeptide.
10.1039/C3SC51824H
Cited By :26
Export Date: 25 May 2018
The following values have no corresponding Zotero field: publisher: The Royal Society of Chemistry

Synthesis of peptide thioacids at neutral pH using bis(2-sulfanylethyl)amido peptide precursors - Pira, S. L.; Boll, E.; Melnyk, O. (Org. Lett., 2013)
Reaction of bis(2-sulfanylethyl)amido (SEA) peptides with triisopropylsilylthiol in water at neutral pH yields peptide thiocarboxylates. An alkylthioester derived from beta-alanine was used to trap the released bis(2-sulfanylethyl)amine and displace the equilibrium toward the peptide thiocarboxylate.
Cited By :13
Export Date: 25 May 2018
Pira, Silvain L Boll, Emmanuelle Melnyk, Oleg Journal article Organic letters Org Lett. 2013 Sep 27.
The following values have no corresponding Zotero field: auth-address: UMR CNRS 8161, Pasteur Institute of Lille 59021 Lille, France. number: 20 edition: 2013/10/01 accession-num: 24073852

C-5'-substituted cinchona alkaloid derivatives catalyse the first highly enantioselective dynamic kinetic resolutions of azlactones by thiolysis - Palacio, Carole; Connon, Stephen J. (Eur. J. Org. Chem., 2013)
The highly enantioselective dynamic kinetic resolution (DKR) of azlactones by thiolysis has been achieved for the first time. Although both the parent alkaloid quinine and known C-5?-urea derivatives fail to promote the reaction effectively, a new class of C-5?-hydroxylated catalysts proved capable of catalysing the DKR of a range of azlactones derived from both unbranched- and, previously challenging, branched-chain amino acids in 84-92 percent ee, including an example of the synthesis of an enantioenriched N-protected thioester derived from an extraterrestrial amino acid isolated from the Murchison meteorite. The highly enantioselective dynamic kinetic resolution (DKR) of azlactones by thiolysis has been achieved for the first time. Although both the parent alkaloid quinine and known C-5?-urea derivatives fail to promote the reaction effectively, a new class of C-5?-hydroxylated catalysts proved capable of catalysing the DKR of a range of azlactones in 84-92 percent ee. Copyright
The following values have no corresponding Zotero field: number: 24
Keywords: #nosource

Highly efficient one-pot ligation and desulfurization - Moyal, Tal; Hemantha, Hosahalli P.; Siman, Peter; Refua, Maya; Brik, Ashraf (Chem. Sci., 2013)
The combination of native chemical ligation and desulfurization is considered a powerful strategy in protein synthesis. Homogeneous desulfurization conditions based on a radical induced reaction have been widely used in the syntheses of various challenging proteins and their analogues. However, the presence of aryl thiols in the reaction mixture as a ligation catalyst hampers one-pot ligation/desulfurization, hence mandating additional purification/lyophilization steps prior to desulfurization. This significantly reduces the yield and prolongs the ligation process. Here we report that the use of preformed peptide-aryl thioester allows for efficient one-pot ligation and desulfurization. This approach was tested successfully for various model peptides including the synthesis of ubiquitin from two fragments. However, in the case of the synthesis of di-ubiquitin chains, where the ligation is mediated by [small delta]-mercaptolysine to form an isopeptide bond, excess aryl thiol was required for efficient ligation, necessitating purification prior to desulfurization. To overcome these obstacles, we found that functionalization of the aryl thiol with a hydrazide moiety enabled, after the ligation step, its capture by resin-aldehyde to permit direct desulfurization. Altogether, these approaches should facilitate protein synthesis with improved efficiency in yields and time.
2041-6520 10.1039/C3SC50239B
The following values have no corresponding Zotero field: number: 6 publisher: The Royal Society of Chemistry

Governing parameters of long-range intramolecular S-to-N acyl transfers within (S)-acyl isopeptides - Monbaliu, Jean-Christophe M.; Dive, Georges; Stevens, Christian V.; Katritzky, Alan R. (J. Chem. Theory Comput., 2015)
doi: 10.1021/ct300830k
The following values have no corresponding Zotero field: number: 2 publisher: American Chemical Society

Exploration of an imide capture/N,N-acyl shift sequence for asparagine native peptide bond formation - Mhidia, R.; Boll, E.; Fecourt, F.; Ermolenko, M.; Ollivier, N.; Sasaki, K.; Crich, D.; Delpech, B.; Melnyk, O. (Bioorg Med Chem, 2013)
Imide capture of a C-terminal peptidylazide with a side-chain thioacid derivative of an N-terminally protected aspartyl peptide leads to the formation of an imide bond bringing the two peptide ends into close proximity. Unmasking of the N(alpha) protecting group and intramolecular acyl migration results in the formation of a native peptide bond to asparagine.
Cited By :14
Export Date: 25 May 2018
Mhidia, Reda Boll, Emmanuelle Fecourt, Fabien Ermolenko, Mikhail Ollivier, Nathalie Sasaki, Kaname Crich, David Delpech, Bernard Melnyk, Oleg England Bioorganic & medicinal chemistry Bioorg Med Chem. 2013 Jun 15;21(12):3479-85. doi: 10.1016/j.bmc.2013.02.053. Epub 2013 Mar 24.
The following values have no corresponding Zotero field: auth-address: CNRS UMR 8161, Univ. Lille Nord de France, Institut Pasteur de Lille, 59021 Lille, France. number: 12 edition: 2013/04/23 accession-num: 23602526

Scalable synthesis of g-thiolysine starting from lysine and a side by side comparison with d-thiolysine in non-enzymatic ubiquitination - Merkx, Remco; de Bruin, Gerjan; Kruithof, Art; van den Bergh, Toine; Snip, Erwin; Lutz, Martin; El Oualid, Farid; Ovaa, Huib (Chem. Sci., 2013)
We developed a scalable synthesis of [gamma]-thiolysine starting straight from lysine. The application of [gamma]-thiolysine was compared to [small delta]-thiolysine in the chemical synthesis of K48 and K33 linked diubiquitin conjugates. Both [gamma]- and [small delta]-thiolysine were found to perform equally efficiently as handles for non-enzymatic ubiquitination.
2041-6520 10.1039/C3SC51599K
The following values have no corresponding Zotero field: number: 12 publisher: The Royal Society of Chemistry

Chemoselective sulfenylation and peptide ligation at tryptophan - Malins, Lara R.; Cergol, Katie M.; Payne, Richard J. (Chem. Sci., 2013)
Peptide ligation-desulfurization chemistry at 2-thiol tryptophan (Trp) is described for the first time. Installation of a thiol auxiliary was achieved through late-stage chemoselective sulfenylation chemistry at the 2-position of the indole ring of Trp either in solution or on solid support, thus abrogating the need for the preparation of a pre-formed thiolated amino acid. Peptides possessing the 2-thiol Trp functionality on the N-terminus were shown to facilitate high yielding ligation reactions with a variety of C-terminal peptide thiophenyl thioesters. Efficient removal of the 2-thiol Trp auxiliary following the ligation reactions was achieved via reductive desulfurization and provided native peptide products in excellent yields. The utility of the methodology was demonstrated in the synthesis of a glycosylated fragment of the N-terminal extracellular domain of the chemokine receptor CXCR1.
2041-6520 10.1039/C3SC51497H
The following values have no corresponding Zotero field: number: 1 publisher: The Royal Society of Chemistry

Peptide ligation-desulfurization chemistry at arginine - Malins, L. R.; Cergol, K. M.; Payne, R. J. (ChemBioChem, 2013)
The utility of a new beta-thiol arginine building block in ligation-desulfurization chemistry has been demonstrated through reactions and kinetic studies with a range of peptide thioesters. Application of the method is highlighted by a one-pot, kinetically controlled, rapid ligation to generate a 7 kDa MUC1 glycopeptide.
Journal Article Research Support, Non-U.S. Gov't Germany a European journal of chemical biology
The following values have no corresponding Zotero field: auth-address: School of Chemistry, The University of Sydney, Sydney, New South Wales 2006, Australia. number: 5 accession-num: 23426906
Keywords: Kinetics; Esters; Sulfhydryl Compounds/*chemistry; Arginine/chemical synthesis/*chemistry; Glycopeptides/chemical synthesis/*chemistry; Mucin-1/chemistry

Total synthesis of daptomycin by cyclization via a chemoselective serine ligation - Lam, H. Y.; Zhang, Y.; Liu, H.; Xu, J.; Wong, C. T.; Xu, C.; Li, X. (J. Am. Chem. Soc., 2013)
A total synthesis of daptomycin, the first natural product antibiotic launched in a generation, was achieved. This convergent synthesis relies on an efficient macrocyclization via a serine ligation to assemble the 31-membered cyclic depsipeptide. The difficult esterification by the nonproteinogenic amino acid kynurenine was accomplished via the esterification of a threonine residue by a suitably protected Trp ester, followed by ozonolysis. This synthesis provides a foundation and framework to prepare varied analogues of daptomycin to establish its structure-activity profile.
Lam, Hiu Yung Zhang, Yinfeng Liu, Han Xu, Jianchao Wong, Clarence T T Xu, Ci Li, Xuechen Research Support, Non-U.S. Gov't United States Journal of the American Chemical Society J Am Chem Soc. 2013 Apr 24;135(16):6272-9. doi: 10.1021/ja4012468. Epub 2013 Apr 16.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, People's Republic of China. number: 16 edition: 2013/04/09 accession-num: 23560543

Rapid Formation of N-Glycopeptides via Cu(II)-Promoted Glycosylative Ligation - Joseph, Ryan; Dyer, Frank Brock; Garner, Philip (Org. Lett., 2013)
doi: 10.1021/ol302961s
The following values have no corresponding Zotero field: number: 4 publisher: American Chemical Society

From Sulfur to Selenium. A New Research Arena in Chemical Biology and Biological Chemistry - Iwaoka, Michio; Kenta, Arai (Current Chem. Biol., 2013)
Since the finding that selenium is an essential micronutrient for our life as well as the discovery of selenocysteine (Sec) as the twenty-first proteinogenic amino acid that is expressed by using the information encoded in genes, research fields in chemical biology and biological chemistry have been expanding to a new paradigm where selenium plays important roles. A number of selenoenzymes, which utilize a selenium atom as the active center, have already been characterized, and their biological functions have been identified. However, the chemistry underlying behind their molecular mechanisms is still not fully understood. On the other hand, selenium is a unique element in organic chemistry because it has lower redox potentials than sulfur, rendering organoselenium compounds attractive in applications to redox catalysts and advanced materials. Moreover, selenium atoms in organic compounds have high affinity toward various polar functional groups located in the proximity, forming weak nonbonded interactions between Se and heteroatoms of main-group elements, such as N, O, halogens, etc. Taking advantage of these characteristic features, we recently demonstrated that applications of selenium to the fields of chemical biology and biological chemistry are quite promising for studying various biological problems, such as molecular design of new antioxidants and characterization of oxidative folding pathways of disulfide-containing proteins. In this review, the recent developments in these fields are summarized, along with our own achievements, from a view point of a paradigm shift from sulfur to selenium. This review is divided into four major sections. After brief introduction, physical chemistry aspects of organic selenium compounds, including bond dissociation energies, redox potentials, conformational propensities, and weak nonbonded interactions, are explained in the first section. In the second section, chemical and biological syntheses of selenium compounds, such as Sec and selenomethionine derivatives, selenopeptides, selenoproteins, and other water-soluble selenium compounds, are described. In the third and fourth sections, recent applications of the selenium compounds to the research fields of chemical biology and biological chemistry, respectively, are summarized. The future scopes are given in Conclusions.
2212-7968/1872-3136
The following values have no corresponding Zotero field: number: 1
Keywords: antioxidants; protein folding; Selenocysteine; selenoenzyme; weak interaction

Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: Organic chemistry applied to synthetic proteins - Haj-Yahya, Najat; Haj-Yahya, Mahmood; Castañeda, Carlos A.; Spasser, Liat; Hemantha, Hosahalli P.; Jbara, Muhammad; Penner, Marlin; Ciechanover, Aaron; Fushman, David; Brik, Ashraf (Angew. Chem. Int. Ed., 2013)
The following values have no corresponding Zotero field: number: 42 publisher: WILEY-VCH Verlag
Keywords: deubiquitinases; peptide ligation; protein synthesis; ubiquitin chains; ubiquitination

Pyramidalization of a carbonyl C atom in (2S)-N-(selenoacetyl)proline methyl ester - Guzei, I. A.; Choudhary, A.; Raines, R. T. (Acta Crystallogr. Sect. E Struct. Rep. Online, 2013)
The title compound, C8H13NO2Se, crystallizes as a non-merohedral twin with an approximate 9:1 component ratio with two symmetry-independent mol-ecules in the asymmetric unit. Our density-functional theory (DFT) computations indicate that the carb-oxy C atom is expected to be slightly pyramidal due to an n--> pi* inter-action, wherein the lone pair (n) of the Se atom overlap with the anti-bonding orbital (pi*) of the carbonyl group. Such pyramidalization is observed in one mol-ecule of the title compound but not the other.
R01 AR044276/AR/NIAMS NIH HHS/United States Journal Article United States
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University of Wisconsin-Madison, 1101 University Ave, Madison, WI 53706-1322, USA. alt-title: Acta crystallographica number: Pt 5 accession-num: 23723945

Total synthesis of human galanin-like peptide through an aspartic acid ligation - Guan, Xiaoyang; Drake, Matthew R.; Tan, Zhongping (Org. Lett., 2013)
doi: 10.1021/ol402984r 1523-7060 doi: 10.1021/ol402984r
The following values have no corresponding Zotero field: number: 24 publisher: American Chemical Society

Total chemical synthesis of fully functional photoactive yellow protein - Gordon, W. R.; Bang, D.; Hoff, W. D.; Kent, S. B. H. (Bioorg. Med. Chem., 2013)
The following values have no corresponding Zotero field: auth-address: Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, USA. alt-title: Bioorganic & medicinal chemistry number: 12 accession-num: 23602622
Keywords: Amino Acid Sequence; Models, Molecular; Molecular Sequence Data; Protein Folding; Bacterial Proteins/*chemical synthesis/chemistry; Photoreceptors, Microbial/*chemical synthesis/chemistry

Solid phase synthesis of peptide-selenoesters - Ghassemian, A.; Vila-Farres, X.; Alewood, P. F.; Durek, T. (Bioorg. Med. Chem., 2013)
The synthesis of proteins by native chemical ligation greatly enhances the application of chemistry to complex molecules such as proteins. The essential building blocks for this approach traditionally have been peptide-thioester segments that are linked chemoselectively in consecutive reactions. By using peptide selenoesters instead of thioesters, the ligation rate can be significantly accelerated permitting couplings at difficult sites and potentially enabling new ligation strategies. To facilitate the routine synthesis of selenoester peptides, a general and straightforward procedure has been developed that generates a suitably functionalized resin from which the desired selenoester peptide can be readily synthesized. This simple approach utilizes readily available and cheap chemical agents and enables production of peptide selenoesters of excellent quality in short time and with high recovery. In addition, the stability of peptide selenoesters was examined under different native chemical ligation conditions and compared to thioesters. Selenoesters are slightly more reactive and more susceptible to hydrolysis and aminolysis than thioesters but sufficiently stable under mildly acidic conditions (pH 6.5). Under these conditions, rapid selenoester-mediated ligation is kinetically favoured.
Ghassemian, Artin Vila-Farres, Xavier Alewood, Paul F Durek, Thomas Research Support, Non-U.S. Gov't England Bioorganic & medicinal chemistry Bioorg Med Chem. 2013 Jun 15;21(12):3473-8. doi: 10.1016/j.bmc.2013.03.076. Epub 2013 Apr 6.
The following values have no corresponding Zotero field: auth-address: Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, St Lucia, Brisbane, Queensland 4072, Australia. number: 12 edition: 2013/04/24 accession-num: 23608106

Rapid formal hydrolysis of peptide-athioesters - Gates, Zachary P.; Stephan, Jules R.; Lee, Dong Jun; Kent, Stephen B. H. (Chem. Commun., 2013)
In the presence of 2-mercaptoethanol peptide-[small alpha]thioesters undergo smooth conversion to their corresponding peptide-[small alpha]carboxylates. This general and operationally simple reaction extends the utility of a promising new strategy for cleaving resin-bound Boc/benzyl-protected peptides without the use of hydrogen fluoride.
1359-7345 10.1039/C2CC38229F
The following values have no corresponding Zotero field: number: 8 publisher: The Royal Society of Chemistry

Sumoylation: a regulatory protein modification in health and disease - Flotho, A.; Melchior, F. (Annu. Rev. Biochem., 2013)
Posttranslational modification with small ubiquitin-related modifier (SUMO) proteins is now established as one of the key regulatory protein modifications in eukaryotic cells. Hundreds of proteins involved in processes such as chromatin organization, transcription, DNA repair, macromolecular assembly, protein homeostasis, trafficking, and signal transduction are subject to reversible sumoylation. Hence, it is not surprising that disease links are beginning to emerge and that interference with sumoylation is being considered for intervention. Here, we summarize basic mechanisms and highlight recent developments in the physiology of sumoylation.
Journal Article Review United States
The following values have no corresponding Zotero field: auth-address: Zentrum fur Molekulare Biologie der Universitat Heidelberg, DKFZ-ZMBH, Heidelberg D-69120, Germany. a.flotho@zmbh.uni-heidelberg.de alt-title: Annual review of biochemistry accession-num: 23746258
Keywords: Animals; Humans; *Sumoylation; Genetic Predisposition to Disease; Proteins/*metabolism; Signal Transduction/*genetics/physiology; Small Ubiquitin-Related Modifier Proteins/*metabolism

Se-(9-Fluorenylmethyl) selenoesters; preparation, reactivity, and use as convenient synthons for selenoacids - Fecourt, F.; Delpech, B.; Melnyk, O.; Crich, D. (Org. Lett., 2013)
Se-(9-Fluorenylmethyl) selenoesters are readily prepared, stable precursors to selenocarboxylates, which they liberate on treatment with DBU. Fm selenoesters are compatible with the use of TFA for the removal of Boc groups and with simple peptide bond forming reactions. Amino acid derived selenocarboxylates condense directly with amines to give amides, react smoothly with isocyanates and isothiocyanates to give amides, and couple with electron-deficient azides also to give amides.
Cited By :4
Export Date: 25 May 2018
Fecourt, Fabien Delpech, Bernard Melnyk, Oleg Crich, David United States Organic letters Org Lett. 2013 Jul 19;15(14):3758-61. doi: 10.1021/ol401677a. Epub 2013 Jul 1.
The following values have no corresponding Zotero field: auth-address: Centre de Recherche de Gif, Institut de Chimie des Substances Naturelles, CNRS, 1 Avenue de la Terrasse, 91190 Gif-sur-Yvette, France. number: 14 edition: 2013/07/03 accession-num: 23815771

Alpha-oxo aldehyde or glyoxylyl group chemistry in peptide bioconjugation - El-Mahdi, O.; Melnyk, O. (Bioconjugate Chem., 2013)
Since the 1990s, alpha-oxo aldehyde or glyoxylic acid chemistry has inspired a vast array of synthetic tools for tailoring peptide or protein structures, for developing peptides endowed with novel physicochemical properties or biological functions, for assembling a large diversity of bioconjugates or hybrid materials, or for designing peptide-based micro or nanosystems. This past decade, important developments have enriched the alpha-oxo aldehyde synthetic tool box in peptide bioconjugation chemistry and explored novel applications. The aim of this review is to give a large overview of this creative field.
Cited By :34
El-Mahdi, Ouafaa Melnyk, Oleg United States Bioconjugate chemistry Bioconjug Chem. 2013 May 15;24(5):735-65. doi: 10.1021/bc300516f. Epub 2013 Apr 11.
Export Date: 25 May 2018
The following values have no corresponding Zotero field: auth-address: Universite Sidi Mohamed Ben Abdellah , Faculte Polydisciplinaire de Taza, Morocco. number: 5 edition: 2013/04/13 accession-num: 23578008

Conformational transferability of the sulfenyl carbonyl group -SC(O)- in cyclic thioesters - Dugarte, Nahir Y.; Erben, Mauricio F.; Hey-Hawkins, Evamarie; Lönnecke, Peter; Stadlbauer, Sven; Ge, Mao-Fa; Li, Yao; Piro, Oscar E.; Echeverria, Gustavo A.; Della Védova, Carlos O. (J. Phys. Chem. A, 2013)
doi: 10.1021/jp4045308 1089-5639 doi: 10.1021/jp4045308
The following values have no corresponding Zotero field: number: 27 publisher: American Chemical Society

Native chemical ligation at Asx-Cys, Glx-Cys: Chemical synthesis and high-resolution X-ray structure of ShK toxin by racemic protein crystallography - Dang, B.; Kubota, T.; Mandal, K.; Bezanilla, F.; Kent, S. B. H. (J. Am. Chem. Soc., 2013)
We have re-examined the utility of native chemical ligation at -Gln/Glu-Cys- [Glx-Cys] and -Asn/Asp-Cys- [Asx-Cys] sites. Using the improved thioaryl catalyst 4-mercaptophenylacetic acid (MPAA), native chemical ligation could be performed at -Gln-Cys- and Asn-Cys- sites without side reactions. After optimization, ligation at a -Glu-Cys- site could also be used as a ligation site, with minimal levels of byproduct formation. However, -Asp-Cys- is not appropriate for use as a site for native chemical ligation because of formation of significant amounts of beta-linked byproduct. The feasibility of native chemical ligation at -Gln-Cys- enabled a convergent total chemical synthesis of the enantiomeric forms of the ShK toxin protein molecule. The d-ShK protein molecule was approximately 50,000-fold less active in blocking the Kv1.3 channel than the l-ShK protein molecule. Racemic protein crystallography was used to obtain high-resolution X-ray diffraction data for ShK toxin. The structure was solved by direct methods and showed significant differences from the previously reported NMR structures in some regions of the ShK protein molecule.
Dang, Bobo Kubota, Tomoya Mandal, Kalyaneswar Bezanilla, Francisco Kent, Stephen B H United States Journal of the American Chemical Society J Am Chem Soc. 2013 Aug 14;135(32):11911-9. doi: 10.1021/ja4046795. Epub 2013 Aug 6.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, University of Chicago , Chicago, Illinois 60637, United States. number: 32 edition: 2013/08/08 accession-num: 23919482

A high-resolution structure that provides insight into coiled-coil thiodepsipeptide dynamic chemistry - Dadon, Z.; Samiappan, M.; Shahar, A.; Zarivach, R.; Ashkenasy, G. (Angew. Chem. Int. Ed., 2013)
Stable and reactive: A crystal structure at 1.35 A of a thioester coiled-coil protein reveals high similarity to all-peptide-bond proteins. In these assemblies, the thioester bonds are kept reactive towards thiol molecules in the mixture. This enables efficient domain exchange between proteins in response to changes in folding conditions or introduction of external templates.
Dadon, Zehavit Samiappan, Manickasundaram Shahar, Anat Zarivach, Raz Ashkenasy, Gonen Research Support, Non-U.S. Gov't Germany Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2013 Sep 16;52(38):9944-7. doi: 10.1002/anie.201303900. Epub 2013 Aug 8.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Ben Gurion University of the Negev, Beer Sheva, 84105 (Israel). number: 38 edition: 2013/08/10 accession-num: 23929823

Diaminodiacid-based solid-phase synthesis of peptide disulfide bond mimics - Cui, Hong-Kui; Guo, Ye; He, Yao; Wang, Feng-Liang; Chang, Hao-Nan; Wang, Yu-Jia; Wu, Fang-Ming; Tian, Chang-Lin; Liu, Lei (Angew. Chem. Int. Ed., 2013)
1521-3773
The following values have no corresponding Zotero field: number: 36 publisher: WILEY-VCH Verlag
Keywords: solid-phase synthesis; biological activity; cyclic peptides; disulfide bonds; β-hairpin structure

Making ends meet: chemically mediated circularization of recombinant proteins - Cowper, B.; Craik, D. J.; Macmillan, D. (ChemBioChem, 2013)
A selective N-->S acyl transfer reaction facilitates semi-synthesis of the plant cyclotide kalata B1 from a linear precursor peptide of bacterial origin, through simple appendage of N-terminal cysteine and a thiol-labile C-terminal Gly-Cys motif. This constitutes the first synthesis of a ribosomally derived circular miniprotein, without recourse to protein splicing elements.
Cowper, Ben Craik, David J Macmillan, Derek Research Support, Non-U.S. Gov't Germany Chembiochem : a European journal of chemical biology Chembiochem. 2013 May 10;14(7):809-12. doi: 10.1002/cbic.201300105. Epub 2013 Apr 4.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University College London, Christopher Ingold Building, 20 Gordon Street, London, WC1H 0AJ, UK. number: 7 edition: 2013/04/06 accession-num: 23559418
Keywords: Cyclization; Cyclotides/*biosynthesis/*chemistry; Recombinant Proteins/biosynthesis/*chemistry/metabolism

An n->p* interaction reduces the electrophilicity of the acceptor carbonyl group - Choudhary, A.; Fry, C. G.; Kamer, K. J.; Raines, R. T. (Chem. Commun., 2013)
Carbonyl-carbonyl (C=O...C'=O') interactions are ubiquitous in both small and large molecular systems. This interaction involves delocalization of a lone pair (n) of a donor oxygen into the antibonding orbital (pi*) of an acceptor carbonyl group. Analyses of high-resolution protein structures suggest that these carbonyl-carbonyl interactions prefer to occur in pairs, that is, one donor per acceptor. Here, the reluctance of the acceptor carbonyl group (C'=O') to engage in more than one n-->pi* electron delocalization is probed using imidazolidine-based model systems with one acceptor carbonyl group and two equivalent donor carbonyl groups. The data indicate that the electrophilicity of the acceptor carbonyl group is reduced when it engages in n-->pi* electron delocalization. This diminished electrophilicity discourages a second n-->pi* interaction with the acceptor carbonyl group.
R01 AR044276/AR/NIAMS NIH HHS/United States Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't England
The following values have no corresponding Zotero field: auth-address: Graduate Program in Biophysics, University of Wisconsin-Madison, 1525 Linden Drive, Madison, WI 53706-1534, USA. alt-title: Chemical communications (Cambridge, England) number: 74 accession-num: 23928794
Keywords: Models, Molecular; Molecular Structure; Oxidation-Reduction; Esters/*chemistry; Electrons; Imidazolidines/chemistry

Chemical bypass of intein-catalyzed N-S acyl shift in protein splicing - Binschik, J.; Mootz, H. D. (Angew. Chem. Int. Ed., 2013)
Binschik, Jens Mootz, Henning D Research Support, Non-U.S. Gov't Germany Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2013 Apr 8;52(15):4260-4. doi: 10.1002/anie.201208863. Epub 2013 Mar 6.
The following values have no corresponding Zotero field: auth-address: Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Str. 2, 48149 Munster, Germany. number: 15 edition: 2013/03/08 accession-num: 23468274
Keywords: Catalysis; *Inteins; Protein Splicing; Proteins/chemical synthesis/*chemistry

Photoactivatable chemokines--controlling protein activity by light - Baumann, L.; Beck-Sickinger, A. G. (Angew. Chem. Int. Ed., 2013)
Journal Article Research Support, Non-U.S. Gov't Germany
The following values have no corresponding Zotero field: auth-address: Universitat Leipzig, Institute of Biochemistry, Bruderstrasse 34, 04103 Leipzig, Germany. alt-title: Angewandte Chemie (International ed number: 36 accession-num: 23744757
Keywords: Humans; Models, Molecular; Chromatography, High Pressure Liquid; *Light; Chemokine CXCL12/chemistry; Chemokines/*chemistry/radiation effects; Jurkat Cells; Luminescent Proteins/*chemistry

Fully convergent chemical synthesis of ester insulin: Determination of the high resolution X-ray structure by racemic protein crystallography - Avital-Shmilovici, Michal; Mandal, Kalyaneswar; Gates, Zachary P.; Phillips, Nelson B.; Weiss, Michael A.; Kent, Stephen B. H. (J. Am. Chem. Soc., 2013)
doi: 10.1021/ja311408y 0002-7863 doi: 10.1021/ja311408y
The following values have no corresponding Zotero field: number: 8 publisher: American Chemical Society

Fast preparation of an N-acetylglucosaminylated peptide segment for the chemoenzymatic synthesis of a glycoprotein - Asahina, Y.; Kanda, M.; Suzuki, A.; Katayama, H.; Nakahara, Y.; Hojo, H. (Org. Biomol. Chem., 2013)
A novel GlcNAc-Asn unit carrying trifluoroacetic acid (TFA)-sensitive O-protecting groups was prepared. The unit was used for the solid-phase peptide synthesis (SPPS) of the N-acetylglucosaminylated emmprin (35-69) thioester via one-step deprotection by TFA combined with the N-alkylcysteine thioesterification method. This segment was used for the synthesis of the first Ig domain (22-104) of emmprin carrying GlcNAc by one-pot ligation with other segments using the thioester method. Finally, the sugar chain was elongated by transglycosylation using glycosynthase to give the Ig domain carrying the disialo- and asialo-complex-type sugar chain.
Asahina, Yuya Kanda, Mika Suzuki, Akemi Katayama, Hidekazu Nakahara, Yoshiaki Hojo, Hironobu England Org Biomol Chem. 2013 Nov 7;11(41):7199-207. doi: 10.1039/c3ob41565a.
The following values have no corresponding Zotero field: auth-address: Department of Applied Biochemistry, Tokai University, Hiratsuka, Kanagawa 259-1292, Japan. alt-title: Organic & biomolecular chemistry number: 41 edition: 2013/09/24 accession-num: 24057089 work-type: Research Support, Non-U.S. Gov't
Keywords: Molecular Structure; Glycosylation; Peptides/*chemical synthesis/*chemistry; Glucosamine/analogs & derivatives/*chemical synthesis/*chemistry; Glycoproteins/*biosynthesis/chemistry; Glycoside Hydrolases/chemistry/*metabolism

Chemoenzymatic synthesis of the immunoglobulin domain of Tim-3 carrying a complex-type N-glycan by using a one-pot ligation - Asahina, Yuya; Kamitori, Shigehiro; Takao, Toshifumi; Nishi, Nozomu; Hojo, Hironobu (Angew. Chem. Int. Ed., 2013)
The following values have no corresponding Zotero field: number: 37 publisher: WILEY-VCH Verlag
Keywords: glycoproteins; ligations; peptide thioester; synthesis design

Investigation of peptide thioester formation via N->Se acyl transfer - Adams, A. L.; Macmillan, D. (J. Pept. Sci., 2013)
Native chemical ligation is widely used for the convergent synthesis of proteins. The peptide thioesters required for this process can be challenging to produce, particularly when using Fmoc-based solid-phase peptide synthesis. We have previously reported a route to peptide thioesters, following Fmoc solid-phase peptide synthesis, via an N-->S acyl shift that is initiated by the presence of a C-terminal cysteine residue, under mildly acidic conditions. Under typical reaction conditions, we occasionally observed significant thioester hydrolysis as a consequence of long reaction times (~48 h) and sought to accelerate the reaction. Here, we present a faster route to peptide thioesters, by replacing the C-terminal cysteine residue with selenocysteine and initiating thioester formation via an N-->Se acyl shift. This modification allows thioester formation to take place at lower temperatures and on shorter time scales. We also demonstrate how application of this strategy also accelerates peptide cyclization, when a linear precursor is furnished with an N-terminal cysteine and C-terminal selenocysteine.
Adams, Anna L Macmillan, Derek England Journal of peptide science : an official publication of the European Peptide Society J Pept Sci. 2013 Feb;19(2):65-73. doi: 10.1002/psc.2469. Epub 2013 Jan 7.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK. number: 2 edition: 2013/01/09 accession-num: 23297044
Keywords: Temperature; Molecular Structure; Peptides/*chemical synthesis/chemistry; Nitrogen/chemistry; Sulfhydryl Compounds/*chemistry; Selenocysteine/*chemistry; Esters/*chemistry; Time Factors

Cysteine promoted C-terminal hydrazinolysis of native peptides and proteins - Adams, A. L.; Cowper, B.; Morgan, R. E.; Premdjee, B.; Caddick, S.; Macmillan, D. (Angew. Chem. Int. Ed., 2013)
Tagging the terminus: N-->S acyl transfer in native peptides and proteins can be reliably intercepted with hydrazine. The method allows selective labeling and ligation, without recourse to the use of protein-splicing elements. NCL=native chemical ligation.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ (United Kingdom). alt-title: Angewandte Chemie (International ed number: 49 accession-num: 24123371
Wellcome Trust/United Kingdom Journal Article Research Support, Non-U.S. Gov't Germany
Keywords: Amino Acid Sequence; Humans; Peptides/*chemistry; Cysteine/*chemistry; Molecular Sequence Data; Proteins/*chemistry; Erythropoietin/chemistry; Glycopeptides/chemistry; Hepcidins/chemistry; Hydrazines/*chemistry; Ubiquitin/chemistry

Synthesis of cyclic peptides and cyclic proteins via ligation of peptide hydrazides - Zheng, J. S.; Tang, S.; Guo, Y.; Chang, H. N.; Liu, L. (ChemBioChem, 2012)
Intramolecular ligation of peptide hydrazides is reported to occur readily, causing the lactamization of fully unprotected peptides in an epimerization-free manner. This method relies on the routine procedures of Fmoc solid-phase peptide synthesis. It can be used to prepare cyclic peptides and cyclic proteins under simpler, mild conditions at lower costs.
Journal Article Research Support, Non-U.S. Gov't Germany a European journal of chemical biology
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University of Science and Technology of China, Hefei 230026, P.R. China. number: 4 accession-num: 22302623
Keywords: Proteins/*chemical synthesis/chemistry; Molecular Structure; Oligopeptides/*chemistry; Cyclization; Hydrazines/*chemistry; Peptides, Cyclic/*chemical synthesis/chemistry

Racemic protein crystallography - Yeates, T. O.; Kent, S. B. H. (Annu. Rev. Biophys., 2012)
Although natural proteins are chiral and are all of one "handedness," their mirror image forms can be prepared by chemical synthesis. This opens up new opportunities for protein crystallography. A racemic mixture of the enantiomeric forms of a protein molecule can crystallize in ways that natural proteins cannot. Recent experimental data support a theoretical prediction that this should make racemic protein mixtures highly amenable to crystallization. Crystals obtained from racemic mixtures also offer advantages in structure determination strategies. The relevance of these potential advantages is heightened by advances in synthetic methods, which are extending the size limit for proteins that can be prepared by chemical synthesis. Recent ideas and results in the area of racemic protein crystallography are reviewed.
R01 GM075993/GM/NIGMS NIH HHS/United States Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Review United States
The following values have no corresponding Zotero field: auth-address: Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095, USA. yeates@mbi.ucla.edu alt-title: Annual review of biophysics accession-num: 22443988
Keywords: Animals; Humans; Stereoisomerism; Proteins/*chemistry; Crystallography, X-Ray; Bacteria/chemistry; Crystallography/*methods

N-to-C sequential ligation using peptidyl N,N-bis(2-mercaptoethyl)amide building blocks - Yang, Renliang; Hou, Wen; Zhang, Xiaohong; Liu, Chuan-Fa (Org. Lett., 2012)
doi: 10.1021/ol2031284 1523-7060 doi: 10.1021/ol2031284
The following values have no corresponding Zotero field: publisher: American Chemical Society

Twin disulfides for orthogonal disulfide pairing and the directed folding of multicyclic peptides - Wu, C.; Leroux, J. C.; Gauthier, M. A. (Nat. Chem., 2012)
Multicyclic peptides are emerging as an exciting platform for drug and targeted ligand discovery owing to their expected greater target affinity/selectivity/stability versus linear or monocyclic peptides. However, although the precise pairing of cysteine residues in proteins is routinely achieved in nature, the rational pairing of cysteine residues within polypeptides is a long-standing challenge for the preparation of multicyclic species containing several disulfide bridges. Here, we present an efficient and straightforward approach for directing the intermolecular and intramolecular pairing of cysteine residues within peptides using a minimal CXC motif. Orthogonal disulfide pairing can be exploited in complex redox media to rationally produce dimeric peptides and bi/tricyclic peptides from fully reduced peptides containing 1-6 cysteine residues. This strategy, which does not rely on extensive manipulation of the primary sequence, post-translational modification or protecting groups, should greatly benefit the development of multicyclic peptide therapeutics and targeting ligands.
The following values have no corresponding Zotero field: auth-address: Swiss Federal Institute of Technology Zurich (ETHZ), Department of Chemistry and Applied Biosciences, Wolfgang-Pauli Strasse 10, HCl J 396.4, 8093 Zurich, Switzerland. alt-title: Nature chemistry number: 12 edition: 2012/11/24 accession-num: 23174986 work-type: Research Support, Non-U.S. Gov't
Wu, Chuanliu Leroux, Jean-Christophe Gauthier, Marc A England Nat Chem. 2012 Dec;4(12):1044-9. doi: 10.1038/nchem.1487. Epub 2012 Oct 28.
Keywords: Amino Acid Sequence; Peptides/*chemistry; Molecular Structure; Molecular Sequence Data; Protein Folding; Cyclization; Disulfides/*chemistry

Click synthesis of ubiquitin dimer analogs to interrogate linkage-specific UBA domain binding - Weikart, N. D.; Sommer, S.; Mootz, H. D. (Chem. Commun., 2012)
A new route to the synthesis of triazole-linked ubiquitin dimers (diUbs) as structural analogs of the seven diUbs is reported. Binding studies with the Lys48-specific UBA domain of the Mud1 protein suggest that they represent functionally suitable surrogates of their native counterparts linked by an isopeptide bond.
The following values have no corresponding Zotero field: auth-address: Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Str. 2, D-48149 Munster, Germany. number: 2 edition: 2011/11/19 accession-num: 22095407
Weikart, Nadine D Sommer, Stefanie Mootz, Henning D Research Support, Non-U.S. Gov't England Chemical communications (Cambridge, England) Chem Commun (Camb). 2012 Jan 7;48(2):296-8. doi: 10.1039/c1cc15834a. Epub 2011 Nov 18.
Keywords: Models, Molecular; Protein Binding; Protein Structure, Tertiary; Binding Sites; Carrier Proteins/chemistry/metabolism; Click Chemistry/*methods; Protein Multimerization; Schizosaccharomyces pombe Proteins/chemistry/metabolism; Schizosaccharomyces/chemistry/metabolism; Ubiquitin/*chemical synthesis/chemistry/*metabolism

At last: erythropoietin as a single glycoform - Wang, P.; Dong, S.; Brailsford, J. A.; Iyer, K.; Townsend, S. D.; Zhang, Q.; Hendrickson, R. C.; Shieh, J.; Moore, M. A.; Danishefsky, S. J. (Angew. Chem. Int. Ed., 2012)
The following values have no corresponding Zotero field: auth-address: Laboratory for Bioorganic Chemistry, Sloan-Kettering Institute for Cancer Research, 1275 York Avenue, New York, NY 10065, USA. number: 46 edition: 2012/09/27 accession-num: 23012228
Wang, Ping Dong, Suwei Brailsford, John A Iyer, Karthik Townsend, Steven D Zhang, Qiang Hendrickson, Ronald C Shieh, JaeHung Moore, Malcolm A S Danishefsky, Samuel J CA28824/CA/NCI NIH HHS/United States HL025848/HL/NHLBI NIH HHS/United States R01 HL025848/HL/NHLBI NIH HHS/United States R37 CA028824/CA/NCI NIH HHS/United States Research Support, N.I.H., Extramural Germany Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2012 Nov 12;51(46):11576-84. doi: 10.1002/anie.201206090. Epub 2012 Sep 25.

Theoretical study on formation of thioesters via O-to-S acyl transfer - Wang, Chen; Guo, Qing-Xiang (Sci. China Chem., 2012)
Peptide thioester preparation via intramolecular O-to-S acyl transfer is a recently developed method for protein chemical synthesis through Fmoc chemistry. Theoretical calculations have been carried out to study the mechanism for the formation of thioesters via O-to-S acyl transfer. It is found that the O-to-S acyl transfer occurs via an anionic stepwise mechanism in which the cleavage of the C-O bond is the rate-limiting step. The side reaction of hydrolysis also proceeds through an anionic stepwise process, and its rate-limiting step is the attack of the hydroxide ion on the carbonyl carbon. Increase of the chain length between the ester O atom and the S atom can increase the energy barrier of the O-to-S acyl transfer. On the other hand, substituents at the Î±-position of the ester can reduce the energy barrier.
1869-1870
The following values have no corresponding Zotero field: number: 10 accession-num: Wang2012

Synthesis of cyclic peptides containing a thioester handle for native chemical ligation - van de Langemheen, Helmus; Brouwer, Arwin J.; Kemmink, Johan; Kruijtzer, John A. W.; Liskamp, Rob M. J. (J. Org. Chem., 2012)
doi: 10.1021/jo3015566 0022-3263 doi: 10.1021/jo3015566
The following values have no corresponding Zotero field: number: 22 publisher: American Chemical Society

Synthesis of a Biologically Active Triazole-Containing Analogue of Cystatin A Through Successive Peptidomimetic Alkyne–Azide Ligations - Valverde, Ibai E.; Lecaille, Fabien; Lalmanach, Gilles; Aucagne, Vincent; Delmas, Agnès F. (Angew. Chem. Int. Ed., 2012)
The following values have no corresponding Zotero field: number: 3 publisher: WILEY-VCH Verlag
Keywords: synthetic methods; proteins; click chemistry; peptidomimetics; proteases

Forging isopeptide bonds using thiol-ene chemistry: site-specific coupling of ubiquitin molecules for studying the activity of isopeptidases - Valkevich, E. M.; Guenette, R. G.; Sanchez, N. A.; Chen, Y. C.; Ge, Y.; Strieter, E. R. (J. Am. Chem. Soc., 2012)
Chemical methods for modifying proteins can enable studies aimed at uncovering biochemical function. Herein, we describe the use of thiol-ene coupling (TEC) chemistry to report on the function of branched (also referred to as forked) ubiquitin trimers. We show how site-specific isopeptide (Nepsilon-Gly-L-homothiaLys) bonds are forged between two molecules of Ub, demonstrating the power of TEC in protein conjugation. Moreover, we demonstrate that the Nepsilon-Gly-L-homothiaLys isopeptide bond is processed to a similar extent by deubiquitinases (DUBs) as that of a native Nepsilon-Gly-L-Lys isopeptide bond, thereby establishing the utility of TEC in the generation of Ub-Ub linkages. TEC is then applied to the synthesis of branched Ub trimers. Interrogation of these branched derivatives with DUBs reveals that the relative orientation of the two Ub units has a dramatic impact on how they are hydrolyzed. In particular, cleavage of K48C-linkages is suppressed when the central Ub unit is also conjugated through K6C, whereas cleavage proceeds normally when the central unit is conjugated through either K11C or K63C. The results of this work presage a role for branched polymeric Ub chains in regulating linkage-selective interactions.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, Wisconsin 53706-1322, USA. number: 16 edition: 2012/04/14 accession-num: 22497214
Valkevich, Ellen M Guenette, Robert G Sanchez, Nicholas A Chen, Yi-chen Ge, Ying Strieter, Eric R Research Support, Non-U.S. Gov't United States Journal of the American Chemical Society J Am Chem Soc. 2012 Apr 25;134(16):6916-9. doi: 10.1021/ja300500a. Epub 2012 Apr 17.
Keywords: Models, Molecular; Peptides/*chemistry; Molecular Structure; Ubiquitin/*chemistry; Sulfhydryl Compounds/*chemistry; Carbon-Nitrogen Lyases/chemistry/*metabolism

Nonenzymatic polymerization of ubiquitin: single-step synthesis and isolation of discrete ubiquitin oligomers - Trang, V. H.; Valkevich, E. M.; Minami, S.; Chen, Y. C.; Ge, Y.; Strieter, E. R. (Angew. Chem. Int. Ed., 2012)
Linked: a method based on thiol-ene chemistry enables the synthesis and purification of ubiquitin oligomers with >/=4 units. This approach, which employs free-radical polymerization, can be applied towards the synthesis of homogeneous Lys6-linked ubiquitin oligomers currently inaccessible by enzymatic methods. By using these chains, one can study their roles in the ubiquitin proteasome system and the DNA damage response pathway.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University of Wisconsin-Madison, 53706, USA. number: 52 edition: 2012/11/20 accession-num: 23161800
Trang, Vivian H Valkevich, Ellen M Minami, Shoko Chen, Yi-Chen Ge, Ying Strieter, Eric R R01 HL096971/HL/NHLBI NIH HHS/United States R01HL096971/HL/NHLBI NIH HHS/United States Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Germany Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2012 Dec 21;51(52):13085-8. doi: 10.1002/anie.201207171. Epub 2012 Nov 19.
Keywords: Humans; Polymerization; Proteasome Endopeptidase Complex/metabolism; Sulfhydryl Compounds/chemistry; Ubiquitin/*metabolism

Advances in proline ligation - Townsend, S. D.; Tan, Z.; Dong, S.; Shang, S.; Brailsford, J. A.; Danishefsky, S. J. (J. Am. Chem. Soc., 2012)
Application of native chemical ligation logic to the case of an N-terminal proline is described. Two approaches were studied. One involved incorporation of a 3R-substituted thiyl-proline derivative. Improved results were obtained from a 3R-substituted selenol function, incorporated in the context of an oxidized dimer.
The following values have no corresponding Zotero field: auth-address: Laboratory for Bioorganic Chemistry, Sloan-Kettering Institute for Cancer Research, 1275 York Avenue, New York, New York 10065, USA. number: 8 edition: 2012/02/16 accession-num: 22332757
Townsend, Steven D Tan, Zhongping Dong, Suwei Shang, Shiying Brailsford, John A Danishefsky, Samuel J CA062948/CA/NCI NIH HHS/United States CA28824/CA/NCI NIH HHS/United States R01 CA028824/CA/NCI NIH HHS/United States R37 CA028824-33/CA/NCI NIH HHS/United States T32 CA062948/CA/NCI NIH HHS/United States Research Support, N.I.H., Extramural United States Journal of the American Chemical Society J Am Chem Soc. 2012 Feb 29;134(8):3912-6. doi: 10.1021/ja212182q. Epub 2012 Feb 15.
Keywords: Stereoisomerism; Molecular Structure; Erythropoietin/chemical synthesis/chemistry; Proline/analogs & derivatives/*chemistry

Ionization state of the catalytic dyad Asp25/25' in the HIV-1 protease: NMR studies of site-specifically 13C labelled HIV-1 protease prepared by total chemical synthesis - Torbeev, V. Y.; Kent, S. B. H. (Org. Biomol. Chem., 2012)
Total chemical synthesis was used to site-specifically (13)C-label active site Asp25 and Asp25' residues in HIV-1 protease and in several chemically synthesized analogues of the enzyme molecule. (13)C NMR measurements were consistent with a monoprotonated state for the catalytic dyad formed by the interacting Asp25, Asp25' side chain carboxyls.
P41 RR002301/RR/NCRR NIH HHS/United States S10 RR008438-01/RR/NCRR NIH HHS/United States P41 GM066326/GM/NIGMS NIH HHS/United States S10 RR002781-01/RR/NCRR NIH HHS/United States S10 RR002781/RR/NCRR NIH HHS/United States S10 RR008438/RR/NCRR NIH HHS/United States Journal Article Research Support, U.S. Gov't, Non-P.H.S. England
The following values have no corresponding Zotero field: auth-address: Institute for Biophysical Dynamics, Department of Chemistry, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA. alt-title: Organic & biomolecular chemistry number: 30 accession-num: 22659831
Keywords: Protein Conformation; Substrate Specificity; Chemistry Techniques, Synthetic; Binding Sites; *Aspartic Acid; *Biocatalysis; Carbon Isotopes; HIV Protease/*chemistry/*metabolism; HIV-1/*enzymology; Isotope Labeling; Molecular Dynamics Simulation; Nuclear Magnetic Resonance, Biomolecular

Chemical synthesis of circular proteins - Tam, J. P.; Wong, C. T. (J. Biol. Chem., 2012)
Circular proteins, once thought to be rare, are now commonly found in plants. Their chemical synthesis, once thought to be difficult, is now readily achievable. The enabling methodology is largely due to the advances in entropic chemical ligation to overcome the entropy barrier in coupling the N- and C-terminal ends of large peptide segments for either intermolecular ligation or intramolecular ligation in end-to-end cyclization. Key elements of an entropic chemical ligation consist of a chemoselective capture step merging the N and C termini as a covalently linked O/S-ester intermediate to permit the subsequent step of an intramolecular O/S-N acyl shift to form an amide. Many ligation methods exploit the supernucleophilicity of a thiol side chain at the N terminus for the capture reaction, which makes cysteine-rich peptides ideal candidates for the entropy-driven macrocyclization. Advances in desulfurization and modification of the thiol-containing amino acids at the ligation sites to other amino acids add extra dimensions to the entropy-driven ligation methods. This minireview describes recent advances of entropy-driven ligation to prepare circular proteins with or without a cysteinyl side chain.
Tam, James P Wong, Clarence T T J Biol Chem. 2012 Aug 3;287(32):27020-5. doi: 10.1074/jbc.R111.323568. Epub 2012 Jun 14.
The following values have no corresponding Zotero field: auth-address: School of Biological Sciences, Nanyang Technological University, Singapore 637551. jptam@ntu.edu.sg alt-title: The Journal of biological chemistry number: 32 edition: 2012/06/16 accession-num: 22700959 work-type: Research Support, Non-U.S. Gov't Review
Keywords: Oxidation-Reduction; Protein Folding; Cyclization; Entropy; Plant Proteins/*chemical synthesis

Chemistry and biology of the ubiquitin signal - Spasser, L.; Brik, A. (Angew. Chem. Int. Ed., 2012)
Ubiquitination is one of the most utilized posttranslational modifications in eukaryotes and is involved in a wide range of cellular processes, but is mostly known as a signal for proteasomal degradation. Recently, it has become clear that the ubiquitin signal is far more complex and is dictated by the ubiquitin component and the substrate. The remarkable diversity of the ubiquitin signaling process has triggered an incredible amount of effort to investigate the role of ubiquitination on biological processes. However, despite more than three decades of studies, several important questions remain unanswered. A major hurdle is the inability to obtain homogeneous ubiquitin bioconjugates in sufficient amounts from cells or by application of the enzymatic machinery. Recent breakthroughs in chemical and semisynthetic strategies, however, offer solutions to these challenges. In this Review, we survey the fundamental biological aspects of the ubiquitin signal and present the emerging non-enzymatic approaches for overcoming these obstacles.
Spasser, Liat Brik, Ashraf Research Support, Non-U.S. Gov't Review Germany Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2012 Jul 9;51(28):6840-62. doi: 10.1002/anie.201200020. Epub 2012 Jun 13.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Ben-Gurion University of the Negev, Beer Sheva, Israel. number: 28 edition: 2012/06/15 accession-num: 22696461
Keywords: Animals; Humans; *Signal Transduction; Ubiquitin/*metabolism; *Protein Processing, Post-Translational; Proteasome Endopeptidase Complex/*metabolism; Ubiquitination

Native chemical ligation at glutamine - Siman, Peter; Karthikeyan, Subramanian Vedhanarayanan; Brik, Ashraf (Org. Lett., 2012)
doi: 10.1021/ol300254y 1523-7060 doi: 10.1021/ol300254y
The following values have no corresponding Zotero field: number: 6 publisher: American Chemical Society

Chemical and semisynthesis of posttranslationally modified proteins - Siman, Peter; Brik, Ashraf (Org. Biomol. Chem., 2012)
Posttranslational modifications of proteins play crucial roles in health and disease by affecting numerous aspects of protein structure, function, stability and sub cellular localization. Yet understanding the effects of these modifications on several of these processes at the molecular level has been hindered by the lack of homogeneously modified proteins obtained via traditional biochemical and molecular biology approaches. Moreover, the preparation of such bioconjugates at a workable level is highly demanding. Recent advances in protein chemistry applying chemical and semisynthetic approaches are becoming increasingly beneficial to overcome these challenges. These methods allow site-specific modifications of a desired protein and afford the product in large quantities for biochemical and structural analyses. In this review, we survey these efforts and their importance in dissecting the role of several posttranslational modifications in various proteins. Several examples are presented where glycosylated, phosphorylated, ubiquitinated, lipidated, acetylated and methylated proteins were prepared.
1477-0520 10.1039/C2OB25149C
The following values have no corresponding Zotero field: number: 30 publisher: The Royal Society of Chemistry

Counterion effects on the denaturing activity of guanidinium cation to protein - Shao, Qiang; Fan, Yubo; Yang, Lijiang; Gao, Yi Qin (J. Chem. Theory Comput., 2012)
doi: 10.1021/ct3002267 1549-9618 doi: 10.1021/ct3002267
The following values have no corresponding Zotero field: number: 11 publisher: American Chemical Society

Chemical synthesis of homogeneous human glycosyl-interferon-beta that exhibits potent antitumor activity in vivo - Sakamoto, I.; Tezuka, K.; Fukae, K.; Ishii, K.; Taduru, K.; Maeda, M.; Ouchi, M.; Yoshida, K.; Nambu, Y.; Igarashi, J.; Hayashi, N.; Tsuji, T.; et al. (J. Am. Chem. Soc., 2012)
Chemical synthesis of homogeneous human glycoproteins exhibiting bioactivity in vivo has been a challenging task. In an effort to overcome this long-standing problem, we selected interferon-beta and examined its synthesis. The 166 residue polypeptide chain of interferon-beta was prepared by covalent condensation of two synthetic peptide segments and a glycosylated synthetic peptide bearing a complex-type glycan of biological origin. The peptides were covalently condensed by native chemical ligation. Selective desulfurization followed by deprotection of the two Cys(Acm) residues gave the target full-length polypeptide chain of interferon-beta bearing either a complex-type sialyl biantennary oligosaccharide or its asialo form. Subsequent folding with concomitant formation of the native disulfide bond afforded correctly folded homogeneous glycosyl-interferon-beta. The chemically synthesized sialyl interferon-beta exhibited potent antitumor activity in vivo.
Sakamoto, Izumi Tezuka, Katsunari Fukae, Kazuhiro Ishii, Kazuyuki Taduru, Keisuke Maeda, Masatoshi Ouchi, Masaki Yoshida, Kenta Nambu, Yuri Igarashi, Jun Hayashi, Naohiro Tsuji, Takashi Kajihara, Yasuhiro J Am Chem Soc. 2012 Mar 28;134(12):5428-31. doi: 10.1021/ja2109079. Epub 2012 Mar 15.
The following values have no corresponding Zotero field: auth-address: Glycotechnology Laboratory, Otsuka Chemical Co, Ltd, Shimogyo-ku, Kyoto, Japan. alt-title: Journal of the American Chemical Society number: 12 edition: 2012/03/13 accession-num: 22404596
Keywords: Amino Acid Sequence; Animals; Humans; Models, Molecular; Cell Line; Molecular Sequence Data; Glycosylation; Mice; Antineoplastic Agents/*chemical synthesis/chemistry/*therapeutic use; Cell Proliferation/drug effects; Interferon-beta/*chemical synthesis/chemistry/*therapeutic use; Neoplasms/drug therapy; Xenograft Model Antitumor Assays

Thioester-isocyanides: versatile reagents for the synthesis of cycle-tail peptides - Rotstein, B. H.; Winternheimer, D. J.; Yin, L. M.; Deber, C. M.; Yudin, A. K. (Chem. Commun., 2012)
A novel class of reagents, thioester isocyanides, have been prepared and applied in the synthesis of peptide macrocycles. The isocyanide part of the molecule is deployed in a multicomponent macrocyclization step. This step is followed by chemoselective peptide ligation at the thioester part of the macrocycle. Our method can now be used for rapid assembly and evaluation of cycle-tail peptides.
Rotstein, Benjamin H Winternheimer, David J Yin, Lois M Deber, Charles M Yudin, Andrei K FRN-79284/Canadian Institutes of Health Research/Canada Research Support, Non-U.S. Gov't England Chemical communications (Cambridge, England) Chem Commun (Camb). 2012 Apr 18;48(31):3775-7. doi: 10.1039/c2cc16027g. Epub 2012 Mar 9.
The following values have no corresponding Zotero field: auth-address: Davenport Research Laboratories, Department of Chemistry, University of Toronto, 80 St. George Street, Toronto, Ontario, Canada M5H 3H5. number: 31 edition: 2012/03/21 accession-num: 22430393
Keywords: Solvents/chemistry; Sulfhydryl Compounds/*chemistry; Esters/*chemistry; Cyclization; Cyanides/*chemistry; Peptides, Cyclic/*chemical synthesis; Propanols/chemistry

Understanding the pKa of redox cysteines: The key role of hydrogen bonding - Roos, Goedele; Foloppe, Nicolas; Messens, Joris (Antioxid. Redox Signal, 2013)
The following values have no corresponding Zotero field: number: 1 publisher: Mary Ann Liebert, Inc., publishers

The dynamic kinetic resolution of azlactones with thiol nucleophiles catalyzed by arylated, deoxygenated cinchona alkaloids - Rodriguez-Docampo, Zaida; Quigley, Cormac; Tallon, Sean; Connon, Stephen J. (J. Org. Chem., 2012)
A significant improvement of the available organocatalytic methods (in terms of product substrate scope and product enantiomeric excess) for the generation of enantioenriched alpha-amino acid thioesters via the dynamic kinetic resolution of azlactones is reported. C-9 arylated cinchona alkaloid catalysts have been found to be considerably superior to other bifunctional alkaloid catalysts as the promoters of this asymmetric process.
The following values have no corresponding Zotero field: number: 5
Keywords: #nosource

Fmoc-Based Synthesis of Peptide Thioacids for Azide Ligations via 2-Cyanoethyl Thioesters - Raz, Richard; Rademann, Jorg (Org. Lett., 2013)
doi: 10.1021/ol302247h
The following values have no corresponding Zotero field: number: 19 publisher: American Chemical Society

Sequential native peptide ligation strategies for total chemical protein synthesis - Raibaut, L.; Ollivier, N.; Melnyk, O. (Chem. Soc. Rev., 2012)
Total chemical synthesis of proteins is usually achieved by assembling unprotected peptide segments using site-specific and chemoselective native peptide ligation methods. Access to large proteins often requires the assembly of at least three segments due to the current limits of solid phase synthesis of individual peptide segments. The aim of this tutorial review is to present the basic concepts and challenges underlying the design of sequential peptide ligation strategies using solution or solid phase chemistry. A special emphasis is given to C-to-N and N-to-C three-segment assembly strategies, which potentially give access to proteins composed of up to 150 amino acid residues.
1460-4744 (Electronic) 0306-0012 (Linking) Journal article
Cited By :117
Export Date: 24 September 2018
The following values have no corresponding Zotero field: auth-address: UMR CNRS 8161, Universite Lille Nord de France, Institut Pasteur de Lille, 1 rue du Pr Calmette, 59021 Lille, France. oleg.melnyk@ibl.fr. number: 21 accession-num: 22935750

Chemical Protein Synthesis by Chemoselective alpha-Ketoacid-Hydroxylamine (KAHA) Ligations with 5-Oxaproline - Pattabiraman, V. R.; Ogunkoya, A. O.; Bode, J. W. (Angew. Chem. Int. Ed., 2012)
Chemoselective ligations of two unprotected protein segments that give a native amide bond are valued reactions for the synthesis of proteins. In their Communication (DOI: 10.1002/anie. 201200907), J. W. Bode et al. show that the alpha-ketoacid-hydroxylamine (KAHA) ligation with 5-oxaproline is an efficient reaction for the synthesis of proteins with unprotected protein segments in aqueous buffers. Prokaryotic ubiquitin-like protein and probable cold shock protein A have been synthesized.
Pattabiraman, Vijaya R Ogunkoya, Ayodele O Bode, Jeffrey W Journal article Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2012 Mar 30. doi: 10.1002/anie.201202064.
The following values have no corresponding Zotero field: edition: 2012/04/05 accession-num: 22473920

Study of chemical ligation via 17-, 18- and 19-membered cyclic transition states - Panda, S. S.; El-Nachef, C.; Bajaj, K.; Al-Youbi, A. O.; Oliferenko, A.; Katritzky, A. R. (Chem. Biol. Drug. Des., 2012)
Unprotected S-acylated cysteine isopeptides containing alpha-, beta- or gamma-amino acid units have been synthesized, and their conversion to native hexapeptides by S- to the N-terminus ligations involving 17-, 18- and 19-membered cyclic transition states have been demonstrated both experimentally and computationally to be more favorable than intermolecular cross-ligations.
Journal Article Research Support, Non-U.S. Gov't England
The following values have no corresponding Zotero field: auth-address: Center for Heterocyclic Compounds, Department of Chemistry, University of Florida, Gainesville, FL 32611-7200, USA. alt-title: Chemical biology & drug design number: 6 accession-num: 22974460
Keywords: Molecular Conformation; Cysteine/*chemistry; Nitrogen/chemistry; Peptides/chemical synthesis/*chemistry; Sulfur/*chemistry

A one-pot three-segment ligation strategy for protein chemical synthesis - Ollivier, N.; Vicogne, J.; Vallin, A.; Drobecq, H.; Desmet, R.; El-Mahdi, O.; Leclercq, B.; Goormachtigh, G.; Fafeur, V.; Melnyk, O. (Angew. Chem. Int. Ed., 2012)
1521-3773
Cited By :73
Export Date: 24 September 2018
The following values have no corresponding Zotero field: number: 1 publisher: WILEY-VCH Verlag
Keywords: native chemical ligation; synthetic methods; proteins; solid-phase synthesis; growth factors

A synthetic approach to a peptide a-thioester from an unprotected peptide through cleavage and activation of a specific peptide bond by N-acetylguanidine - Okamoto, R.; Morooka, K.; Kajihara, Y. (Angew. Chem. Int. Ed., 2012)
A different route to peptide alpha-thioesters through a new peptide-bond-cleavage method at a cysteine residue by S-thiocarbonylation and subsequent treatment with N-acetylguanidine is described. The resultant peptidyl-N-acetylguanidine can be converted into the corresponding peptide alpha-thioester and is also usable as an alternative to a peptide alpha-thioester. This method allows efficient kinetically controlled ligation in the presence of thiols.
1521-3773 (Electronic) 1433-7851 (Linking) Journal Article
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Graduate School of Science, Osaka University, 1-1, Machikaneyama, Toyonaka, Osaka (Japan). rokamoto@chem.sci.osaka-u.ac.jp. number: 1 accession-num: 22095697

Sequential a-ketoacid-hydroxylamine (KAHA) ligations: synthesis of C-terminal variants of the modifier protein UFM1 - Ogunkoya, A. O.; Pattabiraman, V. R.; Bode, J. W. (Angew. Chem. Int. Ed., 2012)
Ogunkoya, Ayodele O Pattabiraman, Vijaya R Bode, Jeffrey W Research Support, Non-U.S. Gov't Germany Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2012 Sep 17;51(38):9693-7. doi: 10.1002/anie.201204144. Epub 2012 Aug 22.
The following values have no corresponding Zotero field: auth-address: Laboratorium fur Organische Chemie, Department of Chemistry and Applied Biosciences, ETH Zurich, Wolfgang Pauli Strasse 10, 8093 Zurich, Switzerland. number: 38 edition: 2012/08/24 accession-num: 22915333

Comparison of the reactivity of b-thiolactones and b-lactones toward ring-opening by thiols and amines - Noel, Amandine; Delpech, Bernard; Crich, David (Org. Biomol. Chem., 2012)
An investigation into the comparative reactivity of simple [small beta]-lactones and [small beta]-thiolactones toward a thiol and a primary amine is reported. A simple 3-mercaptomethyl-2-oxetanone is found to undergo rearrangement in the presence of aqueous base to give the corresponding thietane-3-carboxylic acid rather than the 3-hydroxymethyl-2-thietanone. Implications for the use of [small beta]-thiolactones in bioorganic and medicinal chemistry are discussed.
1477-0520 10.1039/C2OB25640A
The following values have no corresponding Zotero field: number: 32 publisher: The Royal Society of Chemistry

Chemical synthesis of an erythropoietin glycoform containing a complex-type disialyloligosaccharide - Murakami, M.; Okamoto, R.; Izumi, M.; Kajihara, Y. (Angew. Chem. Int. Ed., 2012)
Murakami, Masumi Okamoto, Ryo Izumi, Masayuki Kajihara, Yasuhiro Germany International ed. in English Angew Chem Int Ed Engl. 2012 Apr 10;51(15):3567-72. doi: 10.1002/anie.201109034. Epub 2012 Feb 3.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Graduate School of Science, Osaka University, 1-1, Machikaneyama, Toyonaka, 560-0043 Japan. number: 15 edition: 2012/02/07 accession-num: 22307754 work-type: Research Support, Non-U.S. Gov't
Keywords: Amino Acid Sequence; Catalysis; Glycosylation; Molecular Sequence Annotation; Carbohydrate Sequence; Erythropoietin/*analogs & derivatives/*chemical synthesis; Oligosaccharides/*chemical synthesis/chemistry; Protein Isoforms

A new benzotriazole-mediated stereoflexible gateway to hetero-2,5-diketopiperazines - Monbaliu, Jean-Christophe M.; Hansen, Finn K.; Beagle, Lucas K.; Panzner, Matthew J.; Steel, Peter J.; Todadze, Ekaterina; Stevens, Christian V.; Katritzky, Alan R. (Chem. Eur. J., 2012)
Open chain Cbz-L-aa1-L-Pro-Bt (Bt=benzotriazole) sequences were converted into either the corresponding trans- or cis-fused 2,5-diketopiperazines (DKPs) depending on the reaction conditions. Thermodynamic tandem cyclization/epimerization afforded selectively the corresponding trans-DKPs (69–75 %). Complementarily, tandem deprotection/cyclization led to the cis-DKPs (65–72 %). A representative set of proline-containing cis- and trans-DKPs has been prepared. A mechanistic investigation, based on chiral HPLC, kinetics, and computational studies enabled a rationalization of the results.
1521-3765
The following values have no corresponding Zotero field: number: 9 publisher: WILEY-VCH Verlag
Keywords: peptides; synthetic methods; density functional calculations; diketopiperazines; stereoflexible

Recent trends in Cys- and Ser/Thr-based synthetic strategies for the elaboration of peptide constructs - Monbaliu, J. C.; Katritzky, A. R. (Chem. Commun., 2012)
Recent conceptual advances in the chemical synthesis of peptide constructs are described, encompassing native chemical ligation (i.e. the chemoselective covalent condensation of unprotected peptide segments) and O-, S-acyl isopeptide strategies (i.e. internal O,S-to-N acyl transfer within peptides).
Journal Article England
The following values have no corresponding Zotero field: auth-address: Center for Heterocyclic Compounds, Department of Chemistry, University of Florida, Gainesville, 32611-7200, USA. alt-title: Chemical communications (Cambridge, England) number: 95 accession-num: 23072786
Keywords: Solvents/chemistry; Peptides/*chemical synthesis/chemistry; Cysteine/*chemistry; Sulfur/chemistry; Serine/*chemistry; Esterification; Imines/chemistry; Ionic Liquids/chemistry; Threonine/*chemistry; Water/chemistry

Acid-mediated prevention of aspartimide formation in solid phase peptide synthesis - Michels, Tillmann; Dölling, Rudolf; Haberkorn, Uwe; Mier, Walter (Org. Lett., 2012)
The following values have no corresponding Zotero field: number: 20 publisher: American Chemical Society

Chemical synthesis and X-ray structure of a heterochiral {D-protein antagonist plus vascular endothelial growth factor} protein complex by racemic crystallography - Mandal, K.; Uppalapati, M.; Ault-Riche, D.; Kenney, J.; Lowitz, J.; Sidhu, S. S.; Kent, S. B. H. (Proc. Natl. Acad. Sci. U. S. A., 2012)
Total chemical synthesis was used to prepare the mirror image (D-protein) form of the angiogenic protein vascular endothelial growth factor (VEGF-A). Phage display against D-VEGF-A was used to screen designed libraries based on a unique small protein scaffold in order to identify a high affinity ligand. Chemically synthesized D- and L- forms of the protein ligand showed reciprocal chiral specificity in surface plasmon resonance binding experiments: The L-protein ligand bound only to D-VEGF-A, whereas the D-protein ligand bound only to L-VEGF-A. The D-protein ligand, but not the L-protein ligand, inhibited the binding of natural VEGF(165) to the VEGFR1 receptor. Racemic protein crystallography was used to determine the high resolution X-ray structure of the heterochiral complex consisting of {D-protein antagonist + L-protein form of VEGF-A}. Crystallization of a racemic mixture of these synthetic proteins in appropriate stoichiometry gave a racemic protein complex of more than 73 kDa containing six synthetic protein molecules. The structure of the complex was determined to a resolution of 1.6 A. Detailed analysis of the interaction between the D-protein antagonist and the VEGF-A protein molecule showed that the binding interface comprised a contact surface area of approximately 800 A(2) in accord with our design objectives, and that the D-protein antagonist binds to the same region of VEGF-A that interacts with VEGFR1-domain 2.
RR-15301/RR/NCRR NIH HHS/United States Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. United States
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, USA. alt-title: Proceedings of the National Academy of Sciences of the United States of America number: 37 accession-num: 22927390
Keywords: Amino Acid Sequence; Stereoisomerism; Molecular Sequence Data; Chromatography, High Pressure Liquid; Mass Spectrometry; *Models, Molecular; Circular Dichroism; Crystallography, X-Ray; Bacterial Proteins/genetics; Enzyme-Linked Immunosorbent Assay; Epitope Mapping; Ligands; Multiprotein Complexes/*chemistry/metabolism; Open Reading Frames; Surface Plasmon Resonance; synthesis/*chemistry/genetics/*metabolism; Vascular Endothelial Growth Factor A/*chemical

Design, total chemical synthesis, and X-ray structure of a protein having a novel linear-loop polypeptide chain topology - Mandal, K.; Pentelute, B. L.; Bang, D.; Gates, Z. P.; Torbeev, V. Y.; Kent, S. B. H. (Angew. Chem. Int. Ed., 2012)
Journal Article Research Support, U.S. Gov't, Non-P.H.S. Germany
Journal Article Research Support, U.S. Gov't, Non-P.H.S. Germany
The following values have no corresponding Zotero field: auth-address: Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637, USA. alt-title: Angewandte Chemie (International ed number: 6 accession-num: 22213444
The following values have no corresponding Zotero field: auth-address: Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637, USA. alt-title: Angewandte Chemie (International ed number: 6 accession-num: 22213444
Keywords: Models, Molecular; Stereoisomerism; Peptides/chemical synthesis/chemistry; Models, Chemical; Plant Proteins/*chemical synthesis/*chemistry; Protein Structure, Secondary

Synthesis and utility of beta-selenol-phenylalanine for native chemical ligation-deselenization chemistry - Malins, L. R.; Payne, R. J. (Org. Lett., 2012)
An efficient synthetic route to a suitably protected beta-selenol-phenylalanine derivative from commercially available Garner's aldehyde is described. The incorporation of this building block into peptides and its application in native chemical ligation reactions with peptide thioesters are demonstrated. Ligation products were chemoselectively deselenized (including in the presence of unprotected cysteine residues) to provide native peptides.
Journal Article Research Support, Non-U.S. Gov't United States
The following values have no corresponding Zotero field: auth-address: School of Chemistry, The University of Sydney, NSW 2006, Australia. alt-title: Organic letters number: 12 accession-num: 22642500
Keywords: Molecular Structure; Selenium/*chemistry; Peptides/chemistry; Phenylalanine/*chemical synthesis; Selenium Compounds/*chemical synthesis/chemistry

Protein thioester synthesis enabled by sortase - Ling, Jingjing J.; Policarpo, Rocco L.; Rabideau, Amy E.; Liao, Xiaoli; Pentelute, Bradley L. (J. Am. Chem. Soc., 2012)
Proteins containing a C-terminal thioester are important intermediates in semisynthesis. Currently there is one main method for the synthesis of protein thioesters that relies upon the use of engineered inteins. Here we report a simple strategy, utilizing sortase A, for routine preparation of recombinant proteins containing a C-terminal αthioester. We used our method to prepare two different anthrax toxin cargo proteins: one containing an αthioester and another containing a D-polypeptide segment situated between two protein domains. We show that both variants can translocate through protective antigen pore. This new method to synthesize a protein thioester allows for interfacing of sortase-mediated ligation and native chemical ligation.
The following values have no corresponding Zotero field: number: 26 publisher: American Chemical Society

Ligation of expressed protein alpha-hydrazides via genetic incorporation of an alpha-hydroxy acid - Li, Y. M.; Yang, M. Y.; Huang, Y. C.; Li, Y. T.; Chen, P. R.; Liu, L. (ACS Chem. Biol., 2012)
Expressed protein ligation bridges the gap between synthetic peptides and recombinant proteins and thereby significantly increases the size and complexity of chemically synthesized proteins. Although the intein-based expressed protein ligation method has been extensively used in this regard, the development of new expressed protein ligation methods may improve the flexibility and power of protein semisynthesis. In this study a new alternative version of expressed protein ligation is developed by combining the recently developed technologies of hydrazide-based peptide ligation and genetic code expansion. Compared to the previous intein-based expressed protein ligation method, the new method does not require the use of protein splicing technology and generates recombinant protein alpha-hydrazides as ligation intermediates that are more chemically stable than protein alpha-thioesters. Furthermore, the use of an evolved mutant pyrrolysyl-tRNA synthetase(PylRS), ACPK-RS, from M. barkeri shows an improved performance for the expression of recombinant protein backbone oxoesters. By using HdeA as a model protein we demonstrate that the hydrazide-based method can be used to synthesize proteins with correctly folded structures and full biological activity. Because the PylRS-tRNACUAPyl system is compatible with both prokaryotic and eukaryotic cells,the strategy presented here may be readily expanded to manipulate proteins produced in mammalian cells. The new hydrazide-based method may also supplement the intein-based expressed protein ligation method by allowing for a more flexible selection of ligation site.
Li, Yi-Ming Yang, Mai-Yun Huang, Yi-Chao Li, Yi-Tong Chen, Peng R Liu, Lei ACS Chem Biol. 2012 Jun 15;7(6):1015-22. doi: 10.1021/cb300020s. Epub 2012 Mar 26.
The following values have no corresponding Zotero field: auth-address: Tsinghua-Peking Center for Life Sciences, Department of Chemistry, Tsinghua University, Beijing 100084, China. alt-title: ACS chemical biology number: 6 edition: 2012/03/20 accession-num: 22424086 work-type: Research Support, Non-U.S. Gov't
Keywords: Models, Molecular; Protein Stability; Protein Folding; Protein Engineering/*methods; Escherichia coli Proteins/*chemistry/*genetics/metabolism; Escherichia coli/chemistry/*genetics/metabolism; Gene Expression; Hydrazines/*chemistry/metabolism; Hydroxy Acids/*chemistry/metabolism; Recombinant Proteins/chemistry/genetics/metabolism

Chemistry as an expanding resource in protein science: fully synthetic and fully active human parathyroid hormone-related protein (1-141) - Li, J.; Dong, S.; Townsend, S. D.; Dean, T.; Gardella, T. J.; Danishefsky, S. J. (Angew. Chem. Int. Ed., 2012)
Li, Jianfeng Dong, Suwei Townsend, Steven D Dean, Thomas Gardella, Thomas J Danishefsky, Samuel J CA062948/CA/NCI NIH HHS/United States HL25848/HL/NHLBI NIH HHS/United States Research Support, N.I.H., Extramural Germany Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2012 Dec 3;51(49):12263-7. doi: 10.1002/anie.201207603. Epub 2012 Nov 4.
The following values have no corresponding Zotero field: auth-address: Laboratory for Bioorganic Chemistry, Sloan-Kettering Institute for Cancer Research, 1275 York Avenue, New York, NY 10065, USA. number: 49 edition: 2012/11/06 accession-num: 23124999

Through the looking glass-a new world of proteins enabled by chemical synthesis - Kent, S. B. H.; Sohma, Y.; Liu, S.; Bang, D.; Pentelute, B.; Mandal, K. (J. Pept. Sci., 2012)
'Chemical ligation'--the regioselective and chemoselective covalent condensation of unprotected peptide segments--has enabled the synthesis of polypeptide chains of more than 200 amino acids. An efficient total chemical synthesis of the insulin molecule has been devised on the basis of a key ester-linked intermediate that is chemically converted to fully active human insulin. Enzyme molecules of defined covalent structure and with full enzymatic activity have been prepared and characterized by high-resolution X-ray crystallography. A 'glycoprotein mimetic' of defined chemical structure and with a mass of 50,825 Da, has been prepared and shown to have full biological activity and improved pharmacokinetic properties. D-protein molecules that are the mirror images of proteins found in the natural world have been prepared by total chemical synthesis. Racemic protein mixtures, consisting of the D-enantiomers and L-enantiomers of a protein molecule, form highly ordered centrosymmetric crystals with great ease; this has enabled the determination of the crystal structures of recalcitrant protein molecules. A protein with a novel linear-loop covalent topology of the peptide chain has been designed and synthesized and its structure determined by facile crystallization as the quasi-racemate with the D-form of the native protein molecule.We have developed an optimized total chemical synthesis of biologically active vascular endothelial growth factor-A; total synthesis of the mirror-image protein will be used to systematically develop D-protein antagonists of this important growth factor. The total chemical synthesis of proteins is now a practical reality and enables access to a new world of protein molecules.
Kent, Stephen Sohma, Youhei Liu, Suhuai Bang, Duhee Pentelute, Brad Mandal, Kalyaneswar England J Pept Sci. 2012 Jul;18(7):428-36. doi: 10.1002/psc.2421. Epub 2012 Jun 4.
The following values have no corresponding Zotero field: auth-address: University of Chicago, Chicago, IL 60637, USA. skent@uchicago.edu alt-title: Journal of peptide science : an official publication of the European Peptide Society number: 7 edition: 2012/06/08 accession-num: 22674813 work-type: Review
Keywords: Models, Molecular; Proteins/*chemical synthesis/chemistry; Molecular Structure; Crystallography, X-Ray

Total chemical synthesis of calstabin 2 protein - Jullian, M.; Melnyk, O.; Ferry, G.; Boutin, J. A.; Ronga, L.; Puget, K. (Peptides 2012. Proceedings of the Thirty-second European Peptide Symposium, 2012)
Keywords: #nosource

Elucidating the role of C-terminal post-translational modifications using protein semisynthesis strategies: alpha-synuclein phosphorylation at tyrosine 125 - Hejjaoui, M.; Butterfield, S.; Fauvet, B.; Vercruysse, F.; Cui, J.; Dikiy, I.; Prudent, M.; Olschewski, D.; Zhang, Y.; Eliezer, D.; Lashuel, H. A. (J. Am. Chem. Soc., 2012)
Despite increasing evidence that supports the role of different post-translational modifications (PTMs) in modulating alpha-synuclein (alpha-syn) aggregation and toxicity, relatively little is known about the functional consequences of each modification and whether or not these modifications are regulated by each other. This lack of knowledge arises primarily from the current lack of tools and methodologies for the site-specific introduction of PTMs in alpha-syn. More specifically, the kinases that mediate selective and efficient phosphorylation of C-terminal tyrosine residues of alpha-syn remain to be identified. Unlike phospho-serine and phospho-threonine residues, which in some cases can be mimicked by serine/threonine --> glutamate or aspartate substitutions, there are no natural amino acids that can mimic phospho-tyrosine. To address these challenges, we developed a general and efficient semisynthetic strategy that enables the site-specific introduction of single or multiple PTMs and the preparation of homogeneously C-terminal modified forms of alpha-syn in milligram quantities. These advances have allowed us to investigate, for the first time, the effects of selective phosphorylation at Y125 on the structure, aggregation, membrane binding, and subcellular localization of alpha-syn. The development of semisynthetic methods for the site-specific introduction of single or PTMs represents an important advance toward determining the roles of such modifications in alpha-syn structure, aggregation, and functions in heath and disease.
Hejjaoui, Mirva Butterfield, Sara Fauvet, Bruno Vercruysse, Filip Cui, Jia Dikiy, Igor Prudent, Michel Olschewski, Diana Zhang, Yan Eliezer, David Lashuel, Hilal A AG019391/AG/NIA NIH HHS/United States AG025440/AG/NIA NIH HHS/United States R01 AG019391/AG/NIA NIH HHS/United States R01 AG025440/AG/NIA NIH HHS/United States R37 AG019391/AG/NIA NIH HHS/United States Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't United States Journal of the American Chemical Society J Am Chem Soc. 2012 Mar 21;134(11):5196-210. doi: 10.1021/ja210866j. Epub 2012 Mar 13.
The following values have no corresponding Zotero field: auth-address: Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, Ecole Polytechnique Federale de Lausanne (EPFL), CH-1015 Lausanne, Switzerland. number: 11 edition: 2012/02/22 accession-num: 22339654
Keywords: Amino Acid Sequence; Humans; Phosphorylation; Sequence Alignment; HEK293 Cells; alpha-Synuclein/*biosynthesis/chemistry/metabolism; Cells, Cultured; HeLa Cells; Protein Processing, Post-Translational; Tyrosine/chemistry/*metabolism

Long-range intramolecular S -> N acyl migration: a study of the formation of native peptide analogues via 13-, 15-, and 16-membered cyclic transition states - Ha, K.; Chahar, M.; Monbaliu, J. C.; Todadze, E.; Hansen, F. K.; Oliferenko, A. A.; Ocampo, C. E.; Leino, D.; Lillicotch, A.; Stevens, C. V.; Katritzky, A. R. (J. Org. Chem., 2012)
The intramolecular long-range S --> N acyl migration via 13-, 15-, and 16-membered cyclic transition states to form native tetra- and pentapeptide analogues was studied on S-acylcysteine peptides containing beta- or gamma-amino acids. The pH-dependency study of the acyl migration via a 15-membered cyclic transition state indicated that the reaction is favored at a pH range from 7.0 to 7.6. Experimental observations are supported by structural and computational investigations.
Journal Article Research Support, Non-U.S. Gov't United States
The following values have no corresponding Zotero field: auth-address: Center for Heterocyclic Compounds, Department of Chemistry, University of Florida, Gainesville, Florida 32611-7200, USA. alt-title: The Journal of organic chemistry number: 6 accession-num: 22283871
Keywords: Amino Acid Sequence; Peptides/*chemistry; Molecular Structure; Cysteine/*chemistry; Oligopeptides/*chemistry; Computers, Molecular

A general chemical ligation approach towards isopeptide-linked ubiquitin and ubiquitin-like assay reagents - Geurink, P. P.; El Oualid, F.; Jonker, A.; Hameed, D. S.; Ovaa, H. (ChemBioChem, 2012)
Journal Article Research Support, Non-U.S. Gov't Germany a European journal of chemical biology
The following values have no corresponding Zotero field: auth-address: Division of Cell Biology, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands. number: 2 accession-num: 22213387
Keywords: Amino Acid Sequence; Models, Molecular; Molecular Structure; Molecular Sequence Data; Ubiquitin/*chemistry; *Biological Assay; Fluorescent Dyes/chemistry; Lysine/*chemistry; Peptide Hydrolases/chemistry; Rhodamines/*chemistry

Multivalency as a chemical organization and action principle - Fasting, C.; Schalley, C. A.; Weber, M.; Seitz, O.; Hecht, S.; Koksch, B.; Dernedde, J.; Graf, C.; Knapp, E. W.; Haag, R. (Angew. Chem. Int. Ed., 2012)
Multivalent interactions can be applied universally for a targeted strengthening of an interaction between different interfaces or molecules. The binding partners form cooperative, multiple receptor-ligand interactions that are based on individually weak, noncovalent bonds and are thus generally reversible. Hence, multi- and polyvalent interactions play a decisive role in biological systems for recognition, adhesion, and signal processes. The scientific and practical realization of this principle will be demonstrated by the development of simple artificial and theoretical models, from natural systems to functional, application-oriented systems. In a systematic review of scaffold architectures, the underlying effects and control options will be demonstrated, and suggestions will be given for designing effective multivalent binding systems, as well as for polyvalent therapeutics.
Fasting, Carlo Schalley, Christoph A Weber, Marcus Seitz, Oliver Hecht, Stefan Koksch, Beate Dernedde, Jens Graf, Christina Knapp, Ernst-Walter Haag, Rainer Germany Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2012 Oct 15;51(42):10472-98. doi: 10.1002/anie.201201114. Epub 2012 Sep 5.
The following values have no corresponding Zotero field: auth-address: Institut fur Chemie und Biochemie, Freie Universitat Berlin, Takustrasse 3, 14195 Berlin, Germany. number: 42 edition: 2012/09/07 accession-num: 22952048

Convergent chemical synthesis of proteins by ligation of peptide hydrazides - Fang, Ge-Min; Wang, Jia-Xing; Liu, Lei (Angew. Chem. Int. Ed., 2012)
The following values have no corresponding Zotero field: number: 41 publisher: WILEY-VCH Verlag
Keywords: Peptide; Proteine; Schutzgruppen; Syntheseplanung; Totalsynthesen

Direct characterization of native chemical ligation of peptides on silicon nanowires - Dendane, N.; Melnyk, O.; Xu, T.; Grandidier, B.; Boukherroub, R.; Stievenard, D.; Coffinier, Y. (Langmuir, 2012)
We describe the site-specific and chemoselective immobilization of peptides on hydrogen-terminated silicon nanowires (SiNWs) using native chemical ligation (NCL) (i.e., the reaction of a thioester group with a cysteine moiety to give a stable amide bond). The SiNWs investigated in this work were grown via a vapor-liquid-solid mechanism and functionalized with a thioester moiety. The immobilization of the peptides on the SiNWs was demonstrated by synthesizing peptides with an N-terminal cysteine residue and labeled with tetramethylrhodamine or trifluoromethyl groups that were detected by fluorescence and X-ray photoelectron spectroscopy, respectively. The peptides labeled with tetramethylrhodamine or trifluoromethyl groups for fluorescence or X-ray photoelectron spectroscopy (XPS) detection studies were synthesized with an N-terminal cysteine residue. N-Terminal seryl peptides and carboxy-terminated SiNWs were used as controls to demonstrate the chemoselectivity of the peptide immobilization.
Cited By :5
Dendane, Nabil Melnyk, Oleg Xu, Tao Grandidier, Bruno Boukherroub, Rabah Stievenard, Didier Coffinier, Yannick Langmuir. 2012 Sep 18;28(37):13336-44. doi: 10.1021/la3030217. Epub 2012 Sep 6.
Export Date: 24 September 2018
The following values have no corresponding Zotero field: auth-address: IBL, UMR CNRS 8161, 1 rue du professeur Calmette, Lille, France. alt-title: Langmuir : the ACS journal of surfaces and colloids number: 37 edition: 2012/08/31 accession-num: 22931112 work-type: Research Support, Non-U.S. Gov't
Keywords: Peptides/*chemistry; Molecular Structure; Nanowires/*chemistry; Silicon/*chemistry

Ubiquitin-based probes prepared by total synthesis to profile the activity of deubiquitinating enzymes - de Jong, A.; Merkx, R.; Berlin, I.; Rodenko, B.; Wijdeven, R. H.; El Atmioui, D.; Yalcin, Z.; Robson, C. N.; Neefjes, J. J.; Ovaa, H. (ChemBioChem, 2012)
Epitope-tagged active-site-directed probes are widely used to visualize the activity of deubiquitinases (DUBs) in cell extracts, to investigate the specificity and potency of small-molecule DUB inhibitors, and to isolate and identify DUBs by mass spectrometry. With DUBs arising as novel potential drug targets, probes are required that can be produced in sufficient amounts and to meet the specific needs of a given experiment. The established method for the generation of DUB probes makes use of labor-intensive intein-based methods that have inherent limitations concerning the incorporation of unnatural amino acids and the amount of material that can be obtained. Here, we describe the total chemical synthesis of active-site-directed probes and their application to activity-based profiling and identification of functional DUBs. This synthetic methodology allowed the easy incorporation of desired tags for specific applications, for example, fluorescent reporters, handles for immunoprecipitation or affinity pull-down, and cleavable linkers. Additionally, the synthetic method can be scaled up to provide significant amounts of probe. Fluorescent ubiquitin probes allowed faster, in-gel detection of active DUBs, as compared to (immuno)blotting procedures. A biotinylated probe holding a photocleavable linker enabled the affinity pull-down and subsequent mild, photorelease of DUBs. Also, DUB activity levels were monitored in response to overexpression or knockdown, and to inhibition by small molecules. Furthermore, fluorescent probes revealed differential DUB activity profiles in a panel of lung and prostate cancer cells.
Journal Article Research Support, Non-U.S. Gov't Germany a European journal of chemical biology
The following values have no corresponding Zotero field: auth-address: Division of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands. number: 15 accession-num: 23011887
Keywords: Humans; Solid-Phase Synthesis Techniques; *Ubiquitination; Catalytic Domain; Biotin/chemistry; Biotinylation; Cell Line, Tumor; Endopeptidases/*metabolism; Fluorescent Dyes/chemical synthesis/*chemistry/metabolism; Ubiquitin/*chemistry/*metabolism

Conversion of cysteine into dehydroalanine enables access to synthetic histones bearing diverse post-translational modifications - Chalker, J. M.; Lercher, L.; Rose, N. R.; Schofield, C. J.; Davis, B. G. (Angew. Chem. Int. Ed., 2012)
Biotechnology and Biological Sciences Research Council/United Kingdom Cancer Research UK/United Kingdom Wellcome Trust/United Kingdom Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Germany
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, OX1 3TA, UK. alt-title: Angewandte Chemie (International ed number: 8 accession-num: 22247073
Keywords: Humans; Models, Molecular; Protein Conformation; Protein Processing, Post-Translational; Alanine/*analogs & derivatives/chemistry/genetics/metabolism; Alkylation; Cysteine/*chemistry/genetics/metabolism; Histones/*chemistry/genetics/metabolism

Simplifying native chemical ligation with an N-acylsulfonamide linker - Burlina, F.; Morris, C.; Behrendt, R.; White, P.; Offer, J. (Chem. Commun., 2012)
We report a simplified procedure for the chemical ligation of peptides by using the sulfamylbutyryl linker as a mildly activating group capable of participating in ligation. When the peptidyl N-methylsulfonamide is directly added with excess thiols to ligation reactions, the speed of reaction is comparable to native chemical ligation.
Burlina, Fabienne Morris, Caroline Behrendt, Raymond White, Peter Offer, John MRC_MC_U117592730/Medical Research Council/United Kingdom U117592730/Medical Research Council/United Kingdom England Cambridge, England Chem Commun (Camb). 2012 Mar 7;48(20):2579-81. doi: 10.1039/c2cc15911b. Epub 2012 Jan 31.
The following values have no corresponding Zotero field: auth-address: UPMC Univ Paris 06, CNRS, ENS, UMR 7203 Laboratoire des Biomolecules, 4 place Jussieu, 75005 Paris, France. number: 20 edition: 2012/02/01 accession-num: 22290414 work-type: Research Support, Non-U.S. Gov't
Keywords: Peptides/*chemistry; Molecular Structure; Chromatography, High Pressure Liquid; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sulfhydryl Compounds/chemistry; *Chemistry Techniques, Analytical; Sulfonamides/*chemistry

S- to N-Acyl transfer in S-acylcysteine isopeptides via 9-, 10-, 12-, and 13-membered cyclic transition states - Bol'shakov, O.; Kovacs, J.; Chahar, M.; Ha, K.; Khelashvili, L.; Katritzky, A. R. (J. Pept. Sci., 2012)
The following values have no corresponding Zotero field: auth-address: Center for Heterocyclic Compounds, Department of Chemistry, University of Florida, Gainesville, FL 32611-7200, USA. number: 11 accession-num: 23065784
Keywords: Peptides/*chemistry; Molecular Structure; Cysteine/*chemistry; Chromatography, High Pressure Liquid; Acylation; Computer Simulation; Dimerization; Disulfides/chemistry; Peptides, Cyclic/*chemistry

Access to cyclic or branched peptides using bis(2-sulfanylethyl)amido side-chain derivatives of Asp and Glu - Boll, E.; Dheur, J.; Drobecq, H.; Melnyk, O. (Org. Lett., 2012)
Bis(2-sulfanylethyl)amido (SEA) side-chain derivatives of aspartic and glutamic acids enable the synthesis of tail-to-side chain cyclic or branched peptides using standard Fmoc-SPPS followed by SEA native peptide ligation.
1523-7052 (Electronic) 1523-7052 (Linking) Journal Article
The following values have no corresponding Zotero field: auth-address: CNRS UMR 8161, Universite Lille Nord de France, Institut Pasteur de Lille, 59021, Lille, France. number: 9 accession-num: 22537053

Native chemical ligation of thioamide-containing peptides: development and application to the synthesis of labeled alpha-synuclein for misfolding studies - Batjargal, S.; Wang, Y. J.; Goldberg, J. M.; Wissner, R. F.; Petersson, E. J. (J. Am. Chem. Soc., 2012)
Thioamide modifications of the peptide backbone are used to perturb secondary structure, to inhibit proteolysis, as photoswitches, and as spectroscopic labels. Thus far, their incorporation has been confined to single peptides synthesized on solid phase. We have generated thioamides in C-terminal thioesters or N-terminal Cys fragments and examined their compatibility with native chemical ligation conditions. Most sequence variants can be coupled in good yields with either TCEP or DTT as the reductant, though some byproducts are observed with prolonged TCEP incubations. Furthermore, we find that thioamides are compatible with thiazolidine protection of an N-terminal Cys, so that multiple ligations can be used to construct larger proteins. Since the acid-lability of the thioamide prohibits on-resin thioester synthesis using Boc chemistry, we devised a method for the synthesis of thioamide peptides with a masked C-terminal thioester that is revealed in situ. Finally, we have shown that thioamidous peptides can be coupled to expressed protein fragments to generate large proteins with backbone thioamide labels by synthesizing labeled versions of the amyloid protein alpha-synuclein for protein folding studies. In a proof-of-principle experiment, we demonstrated that quenching of fluorescence by thioamides can be used to track conformational changes during aggregation of labeled alpha-synuclein.
S10 RR023444/RR/NCRR NIH HHS/United States RR-023444/RR/NCRR NIH HHS/United States Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. United States
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University of Pennsylvania, Philadelphia, 19104-6323, United States. alt-title: Journal of the American Chemical Society number: 22 accession-num: 22468862
Keywords: Models, Molecular; Peptides/*chemical synthesis/chemistry; *Staining and Labeling; Protein Folding; alpha-Synuclein/*chemistry; Thioamides/*chemistry

Towards the simplification of protein synthesis: iterative solid-supported ligations with concomitant purifications - Aucagne, V.; Valverde, I. E.; Marceau, P.; Galibert, M.; Dendane, N.; Delmas, A. F. (Angew. Chem. Int. Ed., 2012)
Please release me: a new linker for the temporary tagging of peptides at their N-terminus after solid-phase elongation, and its potential for capture/release purification is demonstrated. This concept is extended to a remarkably efficient self-purifying N-to-C iterative triazole ligation strategy, which is applied to the synthesis of a polypeptide having 160 residues, in a high purity without the need for chromatographic purification (orange blocks: peptide segments).
Aucagne, Vincent Valverde, Ibai E Marceau, Philippe Galibert, Mathieu Dendane, Nabil Delmas, Agnes F Research Support, Non-U.S. Gov't Germany Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2012 Nov 5;51(45):11320-4. doi: 10.1002/anie.201206428. Epub 2012 Oct 10.
The following values have no corresponding Zotero field: auth-address: Centre de Biophysique Moleculaire, CNRS UPR, Orleans, France. aucagne@cnrs-orleans.fr number: 45 edition: 2012/10/12 accession-num: 23055459

Convergent synthesis of aminomethylene peptidomimetics - Assem, N.; Yudin, A. K. (Nat Protoc, 2012)
This protocol describes a convergent synthesis of reduced amide bond peptidomimetics using thioacid-terminated peptides and aziridine-containing peptide conjugates. This approach could be used to produce peptides and proteins with modified backbones. The peptide conjugates are made using readily available aziridine aldehydes. The convergent synthesis of peptidomimetics is demonstrated through the preparation of long and short peptide fragments with an aminomethylene group incorporated within them. This transformation is amenable to the synthesis of peptides with reduced amide bonds at cysteine and alanine. The procedure describes the preparation of each component used and highlights the ease of synthesis of aminomethylene peptidomimetics, and takes about 3 d to complete.
Assem, Naila Yudin, Andrei K Research Support, Non-U.S. Gov't England Nature protocols Nat Protoc. 2012 Jun 14;7(7):1327-34. doi: 10.1038/nprot.2012.066.
The following values have no corresponding Zotero field: auth-address: Davenport Research Laboratories, Department of Chemistry, University of Toronto, Toronto, Ontario, Canada. number: 7 edition: 2012/06/23 accession-num: 22722368
Keywords: Molecular Structure; Chromatography, High Pressure Liquid; Amides/*chemistry; Protein Stability; Protein Engineering/*methods; Aziridines/*chemistry; Oligopeptides; Peptidomimetics/*chemical synthesis/*chemistry

Shedding-generated Met receptor fragments can be routed to either the proteasomal or the lysosomal degradation pathway - Ancot, F.; Leroy, C.; Muharram, G.; Lefebvre, J.; Vicogne, J.; Lemiere, A.; Kherrouche, Z.; Foveau, B.; Pourtier, A.; Melnyk, O.; Giordano, S.; Chotteau-Lelievre, A.; et al. (Traffic, 2012)
The receptor tyrosine kinase Met and its ligand, the hepatocyte growth factor/scatter factor, are essential for embryonic development, whereas deregulation of Met signaling pathways is associated with tumorigenesis and metastasis. The presenilin-regulated intramembrane proteolysis (PS-RIP) is involved in ligand-independent downregulation of Met. This proteolytic process involves shedding of the Met extracellular domain followed by gamma-secretase cleavage, generating labile intracellular fragments degraded by the proteasome. We demonstrate here that upon shedding both generated Met N- and C-terminal fragments are degraded directly in the lysosome, with C-terminal fragments escaping gamma-secretase cleavage. PS-RIP and lysosomal degradation are complementary, because their simultaneous inhibition induces synergistic accumulation of fragments. Met N-terminal fragments associate with the high-affinity domain of HGF/SF, confirming its decoy activity which could be reduced through their routing to the lysosome at the expense of extracellular release. Finally, the DN30 monoclonal antibody inducing Met shedding promotes receptor degradation through induction of both PS-RIP and the lysosomal pathway. Thus, we demonstrate that Met shedding initiates a novel lysosomal degradation which participates to ligand-independent downregulation of the receptor.
Ancot, Frederic Leroy, Catherine Muharram, Ghaffar Lefebvre, Jonathan Vicogne, Jerome Lemiere, Arnaud Kherrouche, Zoulika Foveau, Benedicte Pourtier, Albin Melnyk, Oleg Giordano, Silvia Chotteau-Lelievre, Anne Tulasne, David Research Support, Non-U.S. Gov't Denmark Traffic (Copenhagen, Denmark) Traffic. 2012 Sep;13(9):1261-72. doi: 10.1111/j.1600-0854.2012.01384.x. Epub 2012 Jun 20.
Cited By :21
Export Date: 24 September 2018
The following values have no corresponding Zotero field: auth-address: CNRS UMR 8161, Institut de Biologie de Lille, Institut Pasteur de Lille, Universite de Lille 1, Universite de Lille 2, Lille cedex, France. number: 9 edition: 2012/06/08 accession-num: 22672335
Keywords: Animals; Humans; Proteolysis; Mice; Proteasome Endopeptidase Complex/*metabolism; Cell Line, Tumor; Amyloid Precursor Protein Secretases/antagonists & inhibitors/metabolism; Dogs; Hepatocyte Growth Factor/metabolism; Intracellular Membranes/metabolism; Lysosomes/*enzymology; NIH 3T3 Cells; Presenilins/metabolism; Protease Inhibitors/pharmacology; Proto-Oncogene Proteins c-met/genetics/*metabolism; RNA, Small Interfering

Transamidation of primary amides with amines using hydroxylamine hydrochloride as an inorganic catalyst - Allen, C. L.; Atkinson, B. N.; Williams, J. M. (Angew. Chem. Int. Ed., 2012)
Journal Article Research Support, Non-U.S. Gov't Germany
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK. ca221@bath.ac.uk alt-title: Angewandte Chemie (International ed number: 6 accession-num: 22213128
Keywords: Catalysis; Hydroxylamine/*chemistry; Amines/*chemistry; Magnetic Resonance Spectroscopy; Amides/*chemical synthesis/chemistry

Fmoc synthesis of peptide thioesters without post-chain-assembly manipulation - Zheng, J. S.; Chang, H. N.; Wang, F. L.; Liu, L. (J. Am. Chem. Soc., 2011)
An operationally simple method for the synthesis of peptide thioesters is developed using standard Fmoc solid-phase peptide synthesis procedures. The method relies on the use of a premade enamide-containing amino acid which, in the final TFA cleavage step, renders the desired thioester functionality through an irreversible intramolecular N-to-S acyl transfer.
1520-5126 (Electronic) 0002-7863 (Linking) Journal Article
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology (Ministry of Education), Tsinghua University , Beijing 100084, China. number: 29 accession-num: 21714552

Synthesis of human GLP-1 (7-36) by chemoselective a-ketoacid-hydroxylamine peptide ligation of unprotected fragments - Wu, Jian; Ruiz-Rodriguez, Javier; Comstock, Jeanne M.; Dong, Jesse Z.; Bode, Jeffrey W. (Chem. Sci., 2011)
The synthesis of the bioactive form of human glucagon-like peptide, GLP-1 (7-36), by the chemoselective ligation of two unprotected fragments, a C-terminal peptide [small alpha]-ketoacid with an N-terminal peptide hydroxylamine, is reported. No reagents are required for the ligation and no byproducts are produced. Unprotected glutamic acid, histidine, arginine, lysine, serine, and tyrosine residues do not interfere with the ligation; no side products arising from undesired reactions of the side chains are detected. This synthesis is the first reported example of the application of the [small alpha]-ketoacid-hydroxylamine amide ligation to the synthesis of a complex, unprotected peptide. Its success underscores the potential broad utility of this amide ligation for the synthesis of complex peptides and related targets.
2041-6520 10.1039/C1SC00398D
The following values have no corresponding Zotero field: number: 10 publisher: The Royal Society of Chemistry

Theoretical analysis of the detailed mechanism of native chemical ligation reactions - Wang, Chen; Guo, Qing-Xiang; Fu, Yao (Chem. Asian J., 2011)
1861-471X
The following values have no corresponding Zotero field: number: 5 publisher: WILEY-VCH Verlag
Keywords: chemical ligation; peptides; peptide ligation; density functional calculations; reaction mechanisms

Traceless and Site-Specific Ubiquitination of Recombinant Proteins - Virdee, Satpal; Kapadnis, Prashant B.; Elliott, Thomas; Lang, Kathrin; Madrzak, Julia; Nguyen, Duy P.; Riechmann, Lutz; Chin, Jason W. (Journal of the American Chemical Society, 2014)
doi: 10.1021/ja202799r
The following values have no corresponding Zotero field: number: 28 publisher: American Chemical Society

Application of N-C- or C-N-directed sequential native chemical ligation to the preparation of CXCL14 analogs and their biological evaluation - Tsuji, K.; Shigenaga, A.; Sumikawa, Y.; Tanegashima, K.; Sato, K.; Aihara, K.; Hara, T.; Otaka, A. (Bioorg. Med. Chem., 2011)
CXCL14 is a chemokine that exhibits chemoattractant activity for activated macrophages, immature dendric cells, natural killer cells, and epithelial tumor cells. Its potential role as a metabolic regulator has recently been disclosed. However, a complete understanding of its physiological roles remains elusive. This is partly due to the lack of appropriate CXCL14-based molecular probes to explore the biological functions of CXCL14. In this context, we have developed synthetic protocols that provide access to a wide variety of CXCL14 analogs. Two sequential native chemical ligation (NCL) protocols, which proceed in opposite directions, have been used to assemble CXCL14 analogs from peptide fragments. The first involved a conventional C-N-directed sequential NCL, and afforded wild-type CXCL14. The other used peptide thioacids in N-C-directed elongation, and yielded CXCL14 analogs with molecular diversity at the C-terminal fragment. The CXCL14 analogs prepared showed biological activity on human monocytic leukemia-derived THP-1 cells that was comparable to that of wild-type CXCL14.
1464-3391 (Electronic) 0968-0896 (Linking) Journal Article
The following values have no corresponding Zotero field: auth-address: Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima, Shomachi, Tokushima 770-8505, Japan. number: 13 accession-num: 21658958

MET signalling: principles and functions in development, organ regeneration and cancer - Trusolino, L.; Bertotti, A.; Comoglio, P. M. (Nat. Rev. Mol. Cell Biol., 2011)
The MET tyrosine kinase receptor (also known as the HGF receptor) promotes tissue remodelling, which underlies developmental morphogenesis, wound repair, organ homeostasis and cancer metastasis, by integrating growth, survival and migration cues in response to environmental stimuli or cell-autonomous perturbations. The versatility of MET-mediated biological responses is sustained by qualitative and quantitative signal modulation. Qualitative mechanisms include the engagement of dedicated signal transducers and the subcellular compartmentalization of MET signalling pathways, whereas quantitative regulation involves MET partnering with adaptor amplifiers or being degraded through the shedding of its extracellular domain or through intracellular ubiquitylation. Controlled activation of MET signalling can be exploited in regenerative medicine, whereas MET inhibition might slow down tumour progression.
1471-0080 (Electronic) 1471-0072 (Linking) Journal Article Research Support, Non-U.S. Gov't Review
1471-0080 (Electronic) 1471-0072 (Linking) Journal Article Research Support, Non-U.S. Gov't Review
The following values have no corresponding Zotero field: auth-address: Institute for Cancer Research and Treatment (IRCC), University of Torino Medical School, 10060 Candiolo, Torino, Italy. livio.trusolino@ircc.it number: 12 accession-num: 21102609
The following values have no corresponding Zotero field: auth-address: Institute for Cancer Research and Treatment (IRCC), University of Torino Medical School, 10060 Candiolo, Torino, Italy. livio.trusolino@ircc.it number: 12 accession-num: 21102609
Keywords: Animals; Humans; Models, Molecular; Models, Biological; Animal Structures/metabolism/*physiology; Growth and Development/*genetics/physiology; Neoplasms/etiology/*genetics; Proto-Oncogene Proteins c-met/chemistry/genetics/metabolism/*physiology; Regeneration/*genetics/physiology; Signal Transduction/genetics/physiology

Recombinant protein hydrazides: Application to site-specific protein PEGylation - Thom, Jennifer; Anderson, David; McGregor, Joanne; Cotton, Graham (Bioconjugate Chem., 2011)
Here, we describe a novel method for the site-specific C-terminal PEGylation of recombinant proteins. This general approach exploits chemical cleavage of precursor intein-fusion proteins with hydrazine to directly produce recombinant protein hydrazides. This unique functionality within the protein sequence then facilitates site-specific C-terminal modification by hydrazone-forming ligation reactions. This approach was used to generate folded, site-specifically C-terminal PEGylated IFNalpha2b and IFNbeta1b, which retained excellent antiviral activity, demonstrating the utility of this technology in the PEGylation of therapeutic proteins. As this methodology is straightforward to perform, is compatible with disulfide bonds, and is exclusively selective for the protein C-terminus, it shows great potential as general technology for the site-specific engineering and labeling of recombinant proteins.
The following values have no corresponding Zotero field: number: 6 publisher: American Chemical Society

Expanded click conjugation of recombinant proteins with ubiquitin-like modifiers reveals altered substrate preference of SUMO2-modified Ubc9 - Sommer, S.; Weikart, N. D.; Brockmeyer, A.; Janning, P.; Mootz, H. D. (Angew. Chem. Int. Ed., 2011)
Wrestling with SUMO: the chemical conjugation of proteins with small ubiquitin-like modifiers (SUMO) can be achieved by a copper(I)-catalyzed cycloaddition and unnatural amino acid mutagenesis. This approach overcomes previous restrictions related to the primary sequence of proteins and coupling conditions. Moreover, biochemical data suggests that this triazole linkage presents the modifier in a proper distance and orientation relative to the target protein.
Journal Article Research Support, Non-U.S. Gov't Germany
The following values have no corresponding Zotero field: auth-address: Institute of Biochemistry-University of Muenster, Munster, Germany. alt-title: Angewandte Chemie (International ed number: 42 accession-num: 21898723
Keywords: Humans; Substrate Specificity; Click Chemistry; Recombinant Proteins/chemistry/metabolism; Small Ubiquitin-Related Modifier Proteins/chemistry/*metabolism; Ubiquitin-Conjugating Enzymes/chemistry/*metabolism

Synthesis of an O-acyl isopeptide by using native chemical ligation to efficiently construct a hydrophobic polypeptide - Sohma, Youhei; Kitamura, Hitomi; Kawashima, Hiroyuki; Hojo, Hironobu; Yamashita, Masayuki; Akaji, Kenichi; Kiso, Yoshiaki (Tetrahedron Lett., 2011)
By using dimethylformamide to suppress the O-to-N acyl migration, we efficiently synthesized an O-acyl isopeptide by native chemical ligation of a peptide-thioester and a Cys-O-acyl isopeptide. The reaction mixture was then loaded onto an octadecylsilane reverse-phase HPLC column, and the isopeptide was purified by using a linear gradient of CH3CN in 0.1% aqueous trifluoroacetic acid. The recovery rate of the O-acyl isopeptide was considerably higher than that of the corresponding native polypeptide. Synthesis of O-acyl isopeptides via native chemical ligation, with O-to-N acyl migration as the final step to give the native form, has potential as an efficient method of constructing hydrophobic polypeptides.
0040-4039
The following values have no corresponding Zotero field: number: 52
Keywords: Native chemical ligation; HPLC; Hydrophobic peptide; O-Acyl isopeptide; Purification

Histone fold modifications control nucleosome unwrapping and disassembly - Simon, M.; North, J. A.; Shimko, J. C.; Forties, R. A.; Ferdinand, M. B.; Manohar, M.; Zhang, M.; Fishel, R.; Ottesen, J. J.; Poirier, M. G. (Proc Natl Acad Sci U S A, 2011)
Nucleosomes are stable DNA-histone protein complexes that must be unwrapped and disassembled for genome expression, replication, and repair. Histone posttranslational modifications (PTMs) are major regulatory factors of these nucleosome structural changes, but the molecular mechanisms associated with PTM function remains poorly understood. Here we demonstrate that histone PTMs within distinct structured regions of the nucleosome directly regulate the inherent dynamic properties of the nucleosome. Precise PTMs were introduced into nucleosomes by chemical ligation. Single molecule magnetic tweezers measurements determined that only PTMs near the nucleosome dyad increase the rate of histone release in unwrapped nucleosomes. In contrast, FRET and restriction enzyme analysis reveal that only PTMs throughout the DNA entry-exit region increase unwrapping and enhance transcription factor binding to nucleosomal DNA. These results demonstrate that PTMs in separate structural regions of the nucleosome control distinct dynamic events, where the dyad regulates disassembly while the DNA entry-exit region regulates unwrapping. These studies are consistent with the conclusion that histone PTMs may independently influence nucleosome dynamics and associated chromatin functions.
1091-6490 (Electronic) 0027-8424 (Linking) Journal Article
The following values have no corresponding Zotero field: auth-address: Department of Physics, Department of Biochemistry, The Ohio State Biochemistry Program, and The Ohio State Biophysics Graduate Program, The Ohio State University, Columbus, OH 43210. number: 31 accession-num: 21768347

Chemical synthesis and expression of the HIV-1 Rev protein - Siman, P.; Blatt, O.; Moyal, T.; Danieli, T.; Lebendiker, M.; Lashuel, H. A.; Friedler, A.; Brik, A. (ChemBioChem, 2011)
The HIV-1 Rev protein is responsible for shuttling partially spliced and unspliced viral mRNA out of the nucleus. This is a crucial step in the HIV-1 lifecycle, thus making Rev an attractive target for the design of anti-HIV drugs. Despite its importance, there is a lack of structural, biophysical, and quantitative information about Rev. This is mainly because of its tendency to undergo self-assembly and aggregation; this makes it very difficult to express and handle. To address this knowledge gap, we have developed two new highly efficient and reproducible methods to prepare Rev in large quantities for biochemical and structural studies: 1) Chemical synthesis by using native chemical ligation coupled with desulfurization. Notably, we have optimized our synthesis to allow for a one-pot approach for the ligation and desulfurization steps; this reduced the number of purification steps and enabled the obtaining of desired protein in excellent yield. Several challenges emerged during the design of this Rev synthesis, such as racemization, reduced solubility, formylation during thioester synthesis, and the necessity for using orthogonal protection during desulfurization; solutions to these problems were found. 2) A new method for expression and purification by using a vector that contained an HLT tag, followed by purification with a Ni column, a cation exchange column, and gel filtration. Both methods yielded highly pure and folded Rev. The CD spectra of the synthetic and recombinant Rev proteins were identical, and consistent with a predominantly helical structure. These advances should facilitate future studies that aim at a better understanding of the structure and function of the protein.
Journal Article Research Support, Non-U.S. Gov't Germany a European journal of chemical biology
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Ben-Gurion University of the Negev, Beer Sheva, Israel. number: 7 accession-num: 21488138
Keywords: Molecular Structure; Recombinant Proteins/biosynthesis/chemistry/isolation & purification; rev Gene Products, Human Immunodeficiency Virus/*biosynthesis/*chemical; synthesis/chemistry/isolation & purification

Preparation of fully synthetic histone H3 reveals that acetyl-lysine 56 facilitates protein binding within nucleosomes - Shimko, J. C.; North, J. A.; Bruns, A. N.; Poirier, M. G.; Ottesen, J. J. (J. Mol. Biol., 2011)
Posttranslational modification (PTM) of histones plays a central role in genome regulation. Engineering histones with defined PTMs on one residue or on multiple residues is crucial for understanding their function within nucleosomes and chromatin. We introduce a sequential native chemical ligation strategy that is suitable for the preparation of fully synthetic histone proteins, allowing for site-specific incorporation of varied PTMs throughout the sequence. We demonstrate this method with the generation of histone H3 acetylated at lysine 56 [H3(K56ac)]. H3(K56ac) is essential for transcription, replication, and repair. We examined the influence of H3(K56ac) on the targeting of a model DNA binding factor (LexA) to a site approximately 30 bp within the nucleosome. We find that H3(K56ac) increases LexA binding to its DNA target site by 3-fold at physiological ionic strength. We then demonstrate that H3(K56ac) facilitates LexA binding by increasing DNA unwrapping, not by nucleosome repositioning. Furthermore, we find that H3(K56Q) quantitatively imitates H3(K56ac) function. Together, these studies introduce powerful tools for the analysis of histone PTM functions.
1089-8638 (Electronic) 0022-2836 (Linking) Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.
The following values have no corresponding Zotero field: auth-address: Department of Biochemistry and The Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA. number: 2 accession-num: 21310161
Keywords: Amino Acid Sequence; Protein Conformation; Protein Binding; Molecular Sequence Data; Acetylation; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Protein Processing, Post-Translational; Bacterial Proteins/genetics/*metabolism; DNA/genetics/*metabolism; Fluorescence Resonance Energy Transfer; Histones/*chemical synthesis/*metabolism; Lysine/*chemistry/genetics/metabolism; Nucleosomes/genetics/*metabolism; Peptide Fragments/genetics/metabolism; Serine Endopeptidases/genetics/*metabolism

Hydrazine-sensitive thiol protecting group for peptide and protein chemistry - Shen, F.; Zhang, Z. P.; Li, J. B.; Lin, Y.; Liu, L. (Org. Lett., 2011)
In the search for a new Cys side-chain protecting group that is compatible to the solid-phase peptide synthesis yet can be removed under mild conditions, the Hqm and Hgm groups that are readily deprotected by using aqueous hydrazine have been developed. The utility of these groups for peptide and protein chemistry is tested by the total synthesis of a peptide antibiotic trifolitoxin and the human neutrophil defensin hNP2.
Journal Article Research Support, Non-U.S. Gov't United States
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University of Science and Technology of China, Hefei 230026, China. alt-title: Organic letters number: 4 accession-num: 21235223
Keywords: Humans; Hydrogen-Ion Concentration; Molecular Structure; Peptides/*chemical synthesis/chemistry; Cysteine/*chemistry; Hydrazines/*chemistry; Defensins/*chemical synthesis/chemistry

Direct Fmoc-chemistry-based solid-phase synthesis of peptidyl thioesters - Sharma, Indrajeet; Crich, David (J. Org. Chem., 2011)
The following values have no corresponding Zotero field: number: 16 publisher: American Chemical Society

An advance in proline ligation - Shang, S.; Tan, Z.; Dong, S.; Danishefsky, S. J. (J. Am. Chem. Soc., 2011)
Native chemical ligation (NCL) is widely applicable for building proteins in the laboratory. Since the discovery of this method, many strategies have been developed to enhance its capability and efficiency. Because of the poor reactivity of proline thioesters, ligation at a C-terminal proline site is not readily accomplished. Here, we demonstrate that ligation at an N-terminal protein is feasible using the combined logic of NCL and metal-free dethiylation (MFD).
Shang, Shiying Tan, Zhongping Dong, Suwei Danishefsky, Samuel J CA28824/CA/NCI NIH HHS/United States R01 CA028824/CA/NCI NIH HHS/United States R37 CA028824-33/CA/NCI NIH HHS/United States Research Support, N.I.H., Extramural United States Journal of the American Chemical Society J Am Chem Soc. 2011 Jul 20;133(28):10784-6. doi: 10.1021/ja204277b. Epub 2011 Jun 23.
The following values have no corresponding Zotero field: auth-address: Laboratory for Bioorganic Chemistry, Sloan-Kettering Institute for Cancer Research, 1275 York Avenue, New York, New York 10065, USA. number: 28 edition: 2011/06/24 accession-num: 21696220
Keywords: Stereoisomerism; Sulfur/chemistry; Proline/*chemistry; Proteins/chemical synthesis/chemistry

Application of the logic of cysteine-free native chemical ligation to the synthesis of Human Parathyroid Hormone (hPTH) - Shang, S.; Tan, Z.; Danishefsky, S. J. (Proc. Natl. Acad. Sci. U. S. A., 2011)
The power of chemical synthesis of large cysteine-free polypeptides has been significantly enhanced through the use of nonproteogenic constructs which bear strategically placed thiol groups, enabling native chemical ligation. Central to these much expanded capabilities is the specific, radical-induced, metal-free dethiolation, which can be accomplished in aqueous medium.
CA28824/CA/NCI NIH HHS/United States R01 CA028824/CA/NCI NIH HHS/United States Journal Article Research Support, N.I.H., Extramural United States
The following values have no corresponding Zotero field: auth-address: Bio-Organic Chemistry Laboratory, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10065, USA. alt-title: Proceedings of the National Academy of Sciences of the United States of America number: 15 accession-num: 21444787
Keywords: Amino Acid Sequence; Humans; Cysteine/*chemistry; Molecular Sequence Data; Amino Acid Substitution; Circular Dichroism; Parathyroid Hormone/*chemical synthesis/chemistry

N-sulfanylethylanilide peptide as a crypto-thioester peptide - Sato, K.; Shigenaga, A.; Tsuji, K.; Tsuda, S.; Sumikawa, Y.; Sakamoto, K.; Otaka, A. (ChemBioChem, 2011)
1439-7633 (Electronic) 1439-4227 (Linking) Journal Article
The following values have no corresponding Zotero field: auth-address: Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima, Shomachi, Tokushima 770-8505 (Japan). number: 12 accession-num: 21739560

Chemistry with and around thioacids - Sasaki, Kaname; Aubry, Sylvain; Crich, David (Phosphorus, Sulfur, and Silicon, 2011)
Keywords: #nosource

Ascorbate as an alternative to thiol additives in native chemical ligation - Rohde, H.; Schmalisch, J.; Harpaz, Z.; Diezmann, F.; Seitz, O. (ChemBioChem, 2011)
1439-7633 (Electronic) 1439-4227 (Linking) Journal Article Research Support, Non-U.S. Gov't
The following values have no corresponding Zotero field: auth-address: Institut fur Chemie der Humboldt Universitat zu Berlin, Berlin, Germany. number: 9 accession-num: 21557429
Keywords: Amino Acid Sequence; Peptides/*chemical synthesis/chemistry; Molecular Sequence Data; Sulfhydryl Compounds/chemistry; Ascorbic Acid/*chemistry; Phosphines/chemistry

Fmoc-based synthesis of peptide thioesters for native chemical ligation employing a tert-butyl thiol linker - Raz, R.; Rademann, J. (Org. Lett., 2011)
tert-Butyl thioesters display an astonishing stability toward secondary amines in basic milieu, in contrast to other alkyl and aryl thioesters. Exploiting this enhanced stability, peptide thioesters were synthesized in a direct manner, applying a tert-butyl thiol linker for Fmoc-based solid-phase peptide synthesis.
Raz, Richard Rademann, Jorg Research Support, Non-U.S. Gov't United States Organic letters Org Lett. 2011 Apr 1;13(7):1606-9. doi: 10.1021/ol1029723. Epub 2011 Feb 28.
The following values have no corresponding Zotero field: auth-address: Leibniz Institute of Molecular Pharmacology (FMP), 13125, Germany. number: 7 edition: 2011/03/02 accession-num: 21355617
Keywords: Peptides/*chemistry; Molecular Structure; Sulfhydryl Compounds/*chemistry; Esters/*chemical synthesis

An investigation into the origin of the dramatically reduced reactivity of peptide-prolyl-thioesters in native chemical ligation - Pollock, Samuel B.; Kent, Stephen B. H. (Chem. Commun., 2011)
The low reactivity of peptide-prolyl-thioesters in native chemical ligation is not due to steric effects at the [small beta]-carbon, but rather to the presence of a carbonyl moiety on the nitrogen atom of the proline.
1359-7345
The following values have no corresponding Zotero field: number: 8 publisher: The Royal Society of Chemistry

Rethinking amide bond synthesis - Pattabiraman, V. R.; Bode, J. W. (Nature, 2011)
One of the most important reactions in organic chemistry--amide bond formation--is often overlooked as a contemporary challenge because of the widespread occurrence of amides in modern pharmaceuticals and biologically active compounds. But existing methods are reaching their inherent limits, and concerns about their waste and expense are becoming sharper. Novel chemical approaches to amide formation are therefore being developed. Here we review and summarize a new generation of amide-forming reactions that may contribute to solving these problems. We also consider their potential application to current synthetic challenges, including the development of catalytic amide formation, the synthesis of therapeutic peptides and the preparation of modified peptides and proteins.
Pattabiraman, Vijaya R Bode, Jeffrey W Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review England Nature Nature. 2011 Dec 21;480(7378):471-9. doi: 10.1038/nature10702.
The following values have no corresponding Zotero field: auth-address: Laboratorium fur Organische Chemie, ETH Zurich, 8093 Zurich, Switzerland. number: 7378 edition: 2011/12/24 accession-num: 22193101
Keywords: Amides/*chemistry; *Chemistry Techniques, Synthetic; Organic Chemistry Processes

Alternating chemical ligation reactivity of S-acyl peptides explained with theory and computations - Oliferenko, A. A.; Katritzky, A. R. (Org. Biomol. Chem., 2011)
Previously discovered alternating reactivity of S-acyl di-, tri-, and tetrapeptide in internal chemical ligation reactions is rationalised using conformational search, virtual screening methods and quantum chemical calculations. Conformational preorganisation is shown to be the major controller of reactivity, with hydrogen bonding providing additional stabilisation for the tetrapeptide structure.
Journal Article England
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University of Florida, Gainesville, FL 32611-7200, USA. alt-title: Organic & biomolecular chemistry number: 13 accession-num: 21589988
Keywords: Models, Molecular; Peptides/*chemistry; Hydrogen Bonding; Protein Structure, Tertiary; Models, Chemical; Imaging, Three-Dimensional

Hepatocyte growth factor twenty years on: Much more than a growth factor - Nakamura, T.; Sakai, K.; Matsumoto, K. (J Gastroenterol Hepatol, 2011)
Liver regeneration depends on the proliferation of mature hepatocytes. In the 1980s, the method for the cultivation of mature hepatocytes provided an opportunity for the discovery of hepatocyte growth factor (HGF) as a protein that is structurally and functionally different from other growth factors. In 1991, the scatter factor, tumor cytotoxic factor, and 3-D epithelial morphogen were identified as HGF, and Met tyrosine kinase was identified as the receptor for HGF. Thus, the connection of apparently unrelated research projects rapidly enriched the research on HGF in different fields. The HGF-Met pathway plays important roles in the embryonic development of the liver and the placenta, in the migration of myogenic precursor cells, and in epithelial morphogenesis. The use of tissue-specific knockout mice demonstrated that in mature tissues the HGF-Met pathway plays a critical role in tissue protection and regeneration, and in providing less susceptibility to chronic inflammation and fibrosis. In various injury and disease models, HGF promotes cell survival, regeneration of tissues, and suppresses and improves chronic inflammation and fibrosis. Drug development using HGF has been challenging, but extensive preclinical studies to address its therapeutic effects have provided significant results sufficient for the development of HGF as a biological drug in the regeneration-based therapy of diseases. Clinical trials using recombinant human HGF protein, or HGF genes, are in progress for the treatment of diseases.
Nakamura, Takahiro Sakai, Katsuya Nakamura, Toshikazu Matsumoto, Kunio Historical Article Research Support, Non-U.S. Gov't Review Australia Journal of gastroenterology and hepatology J Gastroenterol Hepatol. 2011 Jan;26 Suppl 1:188-202. doi: 10.1111/j.1440-1746.2010.06549.x.
The following values have no corresponding Zotero field: auth-address: Cancer Research Institute, Kanazawa University, Kakuma-machi, Japan. edition: 2011/01/14 accession-num: 21199531
Keywords: Animals; Humans; Models, Molecular; Protein Conformation; *Signal Transduction; Structure-Activity Relationship; *Cell Proliferation; *Liver Regeneration; Gene Expression Regulation, Developmental; Hepatocyte Growth Factor/chemistry/genetics/history/*metabolism/therapeutic use; Hepatocytes/metabolism; History, 20th Century; History, 21st Century; Liver/embryology/*metabolism/pathology; Morphogenesis; Organogenesis; Proto-Oncogene Proteins c-met/metabolism; Stem Cells/metabolism

Site-specific pKa determination of selenocysteine residues in selenovasopressin by using 77Se NMR spectroscopy - Mobli, Mehdi; Morgenstern, David; King, Glenn F.; Alewood, Paul F.; Muttenthaler, Markus (Angew. Chem. Int. Ed., 2011)
The following values have no corresponding Zotero field: number: 50 publisher: WILEY-VCH Verlag
Keywords: NMR spectroscopy; pKa values; selective alkylation; selenocysteine; selenovasopressin

9-Fluorenylmethoxycarbonyl-based solid-phase synthesis of peptide a-thioesters - Mende, F.; Seitz, O. (Angew. Chem. Int. Ed., 2011)
Peptide thioesters play a key role in convergent protein synthesis strategies such as native chemical ligation, traceless Staudinger ligation, and Ag(+) -mediated thioester ligation. The Boc-based solid-phase synthesis provides a very reliable access to peptide thioesters. However, the acid lability of many peptide modifications and the requirements of most parallel peptide synthesizers call for the milder Fmoc-based solid-phase synthesis. The Fmoc-based synthesis of peptide thioesters is more cumbersome and typically proceeds with lower yields than the synthesis of peptide acids and peptide amides. The success of native chemical ligation and related technologies has sparked intensive research effort devoted to the development of new methods. The recent progress in this rapidly expanding field is reviewed.
1521-3773 (Electronic) 1433-7851 (Linking) Journal Article Research Support, Non-U.S. Gov't
The following values have no corresponding Zotero field: auth-address: Humboldt-Universitat zu Berlin, Institut fur Chemie, Germany. number: 6 accession-num: 21290490

Chemoselectivity in chemical biology: Acyl transfer reactions with sulfur and selenium - McGrath, Nicholas A.; Raines, Ronald T. (Acc. Chem. Res., 2011)
A critical source of insight into biological function is derived from the chemist’s ability to create new covalent bonds between molecules, whether they are endogenous or exogenous to a biological system. A daunting impediment to selective bond formation, however, is the myriad of reactive functionalities present in biological milieu. The high reactivity of the most abundant molecule in biology—water—makes the challenges all the more difficult. We have met these challenges by exploiting the reactivity of sulfur and selenium in acyl transfer reactions. The reactivity of both sulfur and selenium is high compared to that of their chalcogen congener, oxygen. In this Account, we highlight recent developments in this arena, emphasizing contributions from our laboratory. One focus of our research is furthering the chemistry of native chemical ligation (NCL) and expressed protein ligation (EPL), two related processes that enable the synthesis and semisynthesis of proteins. These techniques exploit the lower pK(a) of thiols and selenols relative to alcohols. Although a deprotonated hydroxyl group in the side chain of a serine residue is exceedingly rare in a biological context, the pK(a) value of the thiol in cysteine (8.5) and of the selenol in selenocysteine (5.7) often render these side chains anionic under physiological conditions. NCL and EPL take advantage of the high nucleophilicity of the thiolate as well as its utility as a leaving group, and we have expanded the scope of these methods to include selenocysteine. Although the genetic code limits the components of natural proteins to 20 or so α-amino acids, NCL and EPL enable the semisynthetic incorporation of a limitless variety of nonnatural modules into proteins. These modules are enabling chemical biologists to interrogate protein structure and function with unprecedented precision. We are also pursuing the further development of the traceless Staudinger ligation, through which a phosphinothioester and azide form an amide. We first reported this chemical ligation method, which leaves no residual atoms in the product, in 2000. Our progress in effecting the reaction in water, without an organic co-solvent, was an important step in the expansion of its utility. Moreover, we have developed the traceless Staudinger reaction as a means for immobilizing proteins on a solid support, providing a general method of fabricating microarrays that display proteins in a uniform orientation. Along with NCL and EPL, the traceless Staudinger ligation has made proteins more readily accessible targets for chemical synthesis and semisynthesis. The underlying acyl transfer reactions with sulfur and selenium provide an efficient means to synthesize, remodel, and immobilize proteins, and they have enabled us to interrogate biological systems.
1520-4898 (Electronic) 0001-4842 (Linking) Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.
21639109[pmid] Acc Chem Res
The following values have no corresponding Zotero field: auth-address: Department of Chemistry and Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, USA. number: 9 accession-num: 21639109
The following values have no corresponding Zotero field: number: 9
Keywords: Hydrogen-Ion Concentration; Selenium/*chemistry; Selenocysteine/chemistry/metabolism; Sulfur/*chemistry; Phosphines/chemistry; Ribonuclease, Pancreatic/chemistry/metabolism; Proteins/chemistry/metabolism

Total chemical synthesis of biologically active vascular endothelial growth factor - Mandal, K.; Kent, S. B. H. (Angew. Chem. Int. Ed., 2011)
1521-3773 (Electronic) 1433-7851 (Linking) Journal article
The following values have no corresponding Zotero field: auth-address: Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics and, Department of Chemistry, The University of Chicago, Chicago, IL 60637 (USA). number: 35 accession-num: 21744452

A reversible protection strategy to improve Fmoc-SPPS of peptide thioesters by the N-acylurea approach - Mahto, S. K.; Howard, C. J.; Shimko, J. C.; Ottesen, J. J. (ChemBioChem, 2011)
C-terminal peptide thioesters are an essential component of the native chemical ligation approach for the preparation of fully or semisynthetic proteins. However, the efficient generation of C-terminal thioesters by Fmoc solid-phase peptide synthesis remains a challenge. The recent N-acylurea approach to thioester synthesis relies on the deactivation of one amine of 3,4-diaminobenzoic acid (Dbz) during Fmoc SPPS. Here, we demonstrate that this approach results in the formation of side products through the over-acylation of Dbz, particularly when applied to Gly-rich sequences. We find that orthogonal allyloxycarbonyl (Alloc) protection of a single Dbz amine eliminates these side products. We introduce a protected Fmoc-Dbz(Alloc) base resin that may be directly used for synthesis with most C-terminal amino acids. Following synthesis, quantitative removal of the Alloc group allows conversion to the active N-acyl-benzimidazolinone (Nbz) species, which can be purified and converted in situ to thioester under ligation conditions. This method is compatible with the automated preparation of peptide-Nbz conjugates. We demonstrate that Dbz protection improves the synthetic purity of Gly-rich peptide sequences derived from histone H4, as well as a 44-residue peptide from histone H3.
1439-7633 (Electronic) 1439-4227 (Linking) Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.
The following values have no corresponding Zotero field: auth-address: Department of Biochemistry, The Ohio State University, Columbus, OH 43210, USA. number: 16 accession-num: 21910203
Keywords: Amino Acid Sequence; Peptides/*chemical synthesis/chemistry; Molecular Sequence Data; Acylation; Solid-Phase Synthesis Techniques; Esters; Sulfhydryl Compounds/chemistry; Aminobenzoic Acids/chemistry; Urea/*chemistry

Synthesis of cyclic peptides through an intramolecular amide bond rearrangement - Macmillan, Derek; De Cecco, Martin; Reynolds, Natalie L.; Santos, Luiz F. A.; Barran, Perdita E.; Dorin, Julia R. (ChemBioChem, 2011)
The following values have no corresponding Zotero field: number: 14 publisher: WILEY-VCH Verlag
Keywords: native chemical ligation; cyclic peptides; acyl transfer; defensin; somatostatin

Use of model peptide reactions for the characterization of kinetically controlled ligation - Lee, J.; Kwon, Y.; Pentelute, B. L.; Bang, D. (Bioconjugate Chem., 2011)
Since the introduction of kinetically controlled ligation (KCL), a chemoselective reaction between a peptide-(alpha)thioarylester and a Cys-peptide-(alpha)thioalkylester, KCL has been utilized for the total chemical synthesis of large proteins (i.e., lysozyme and HIV-protease) by providing fully convergent synthetic routes. Although KCL has the potential to become an important chemistry for protein synthesis, the principle of KCL is not fully characterized. In particular, prior work on KCL has focused on the reactivity difference of the two different -(alpha)thioester forms-alkyl vs aryl. Another equally important feature of KCL, Xaa-Cys ligation sites, has not been investigated. The work reported here describes combinatorial KCL reactions using model peptides to dissect the interplay of the Xaa(1), Xaa(2), -(alpha)thioarylester, and -(alpha)thioalkylester. Results from these studies provide fundamental insights into the KCL reaction, and will lead to the optimal synthetic route for the routine chemical synthesis of large target protein molecules.
1520-4812 (Electronic) 1043-1802 (Linking) Journal Article Research Support, Non-U.S. Gov't
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Yonsei University, Shinchon 134 Seoul 120-749 Korea. number: 8 accession-num: 21740060
Keywords: Kinetics; Peptides/*chemistry; Proteins/*chemical synthesis; Esterification; Combinatorial Chemistry Techniques; HIV Protease/chemical synthesis; Methods; Muramidase/chemical synthesis

Total chemical synthesis of an integral membrane enzyme: diacylglycerol kinase from Escherichia coli - Lahiri, S.; Brehs, M.; Olschewski, D.; Becker, C. F. (Angew. Chem. Int. Ed., 2011)
1521-3773 (Electronic) 1433-7851 (Linking) Journal Article Research Support, Non-U.S. Gov't
The following values have no corresponding Zotero field: auth-address: Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany. number: 17 accession-num: 21433227

Total chemical synthesis of di-ubiquitin chains - Kumar, K. S.; Spasser, L.; Erlich, L. A.; Bavikar, S. N.; Brik, A. (Angew. Chem. Int. Ed., 2011)
1521-3773 (Electronic) 1433-7851 (Linking) Journal Article Research Support, Non-U.S. Gov't
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Ben-Gurion University of the Negev, Beer Sheva 84105, Israel. number: 48 accession-num: 20815002
Keywords: Amino Acid Sequence; Humans; Models, Molecular; Molecular Sequence Data; Polyubiquitin/*chemical synthesis/*chemistry

Total chemical synthesis of a 304 amino acid K48-linked tetraubiquitin protein - Kumar, K. S.; Bavikar, S. N.; Spasser, L.; Moyal, T.; Ohayon, S.; Brik, A. (Angew. Chem. Int. Ed., 2011)
1521-3773 (Electronic) 1433-7851 (Linking) Journal Article
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Ben-Gurion University of the Negev, Beer Sheva 84105 (Israel), Fax: (+972) 8-6472943 http://www.bgu.ac.il/ approximately abrik. number: 27 accession-num: 21591043

Structural basis for ligand recognition and discrimination of a quorum-quenching antibody - Kirchdoerfer, R. N.; Garner, A. L.; Flack, C. E.; Mee, J. M.; Horswill, A. R.; Janda, K. D.; Kaufmann, G. F.; Wilson, I. A. (J. Biol. Chem., 2011)
In the postantibiotic era, available treatment options for severe bacterial infections caused by methicillin-resistant Staphylococcus aureus have become limited. Therefore, new and innovative approaches are needed to combat such life-threatening infections. Virulence factor expression in S. aureus is regulated in a cell density-dependent manner using "quorum sensing," which involves generation and secretion of autoinducing peptides (AIPs) into the surrounding environment to activate a bacterial sensor kinase at a particular threshold concentration. Mouse monoclonal antibody AP4-24H11 was shown previously to blunt quorum sensing-mediated changes in gene expression in vitro and protect mice from a lethal dose of S. aureus by sequestering the AIP signal. We have elucidated the crystal structure of the AP4-24H11 Fab in complex with AIP-4 at 2.5 A resolution to determine its mechanism of ligand recognition. A key Glu(H95) provides much of the binding specificity through formation of hydrogen bonds with each of the four amide nitrogens in the AIP-4 macrocyclic ring. Importantly, these structural data give clues as to the interactions between the cognate staphylococcal AIP receptors AgrC and the AIPs, as AP4-24H11.AIP-4 binding recapitulates features that have been proposed for AgrC-AIP recognition. Additionally, these structural insights may enable the engineering of AIP cross-reactive antibodies or quorum quenching vaccines for use in active or passive immunotherapy for prevention or treatment of S. aureus infections.
CA058896/CA/NCI NIH HHS/United States AI078921/AI/NIAID NIH HHS/United States R01 CA058896/CA/NCI NIH HHS/United States AI080715/AI/NIAID NIH HHS/United States R01 AI080715/AI/NIAID NIH HHS/United States R01 AI042266/AI/NIAID NIH HHS/United States R01 AI078921/AI/NIAID NIH HHS/United States R37 AI042266/AI/NIAID NIH HHS/United States AI042266/AI/NIAID NIH HHS/United States Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. United States
The following values have no corresponding Zotero field: auth-address: Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA. alt-title: The Journal of biological chemistry number: 19 accession-num: 21454495
Keywords: Models, Molecular; Protein Binding; Peptides/chemistry; Crystallography, X-Ray/methods; *Ligands; Bacterial Proteins/chemistry/metabolism; Gene Expression Regulation, Bacterial; Immunoglobulin Fragments/chemistry; Immunoglobulin G/chemistry; Luminescent Proteins/metabolism; Protein Interaction Mapping; Quorum Sensing/*genetics/immunology; Signal Transduction; Staphylococcus aureus/*genetics

Chemical ligation of S-acylated cysteine peptides to form native peptides via 5-, 11-, and 14-membered cyclic transition states - Katritzky, A. R.; Tala, S. R.; Abo-Dya, N. E.; Ibrahim, T. S.; El-Feky, S. A.; Gyanda, K.; Pandya, K. M. (J. Org. Chem., 2011)
Cysteine-containing dipeptides 3a-l, (3b+3b') (compound numbers in parentheses are used to indicate racemic mixtures; thus (3b+3b') is the racemate of 3b and 3b'), and tripeptide 13 were synthesized in 68-96% yields by acylation of cysteine with N-(Pg-alpha-aminoacyl)- and N-(Pg-alpha-dipeptidoyl)benzotriazoles (where Pg stands for protecting group in the nomenclature for peptides throughout the paper) in the presence of Et(3)N. Cysteine-containing peptides 3a-l and 13 were S-acylated to give S-(Pg-alpha-aminoacyl)dipeptides 5a-l and S-(Pg-alpha-aminoacyl)tripeptide 14 without racemization in 47-90% yields using N-(Pg-alpha-aminoacyl)benzotriazoles 2 in CH(3)CN-H(2)O (7:3) in the presence of KHCO(3). (In our peptide nomenclature, the prefixes di-, tri-, etc. refer to the number of amino acid residues in the main peptide chain; amino acid residues attached to sulfur are designated as S-acyl peptides. Thus we avoid use of the prefix "iso".) Selective S-acylations of serine peptide 3k and threonine peptide 3l containing free OH groups were thus achieved in 58% and 72% yield, respectively. S-(Pg-alpha-aminoacyl)cysteines 4a,b underwent native chemical ligations to form native dipeptides 3f,i via 5-membered cyclic transition states. Microwave irradiation of S-(Pg-alpha-aminoacyl)tripeptide 15 and S-(Pg-alpha-aminoacyl)tetrapeptide 17 in the presence of NaH(2)PO(4)/Na(2)HPO(4) buffer solution at pH 7.8 achieved chemical ligations, involving intramolecular migrations of acyl groups, via 11- and 14-membered cyclic transition states from the S-atom of a cysteine residue to a peptide terminal amino group to form native peptides 19 and 20 in isolated yields of 26% and 23%, respectively.
Journal Article United States
The following values have no corresponding Zotero field: auth-address: Center for Heterocyclic Compounds, Department of Chemistry, University of Florida, Gainesville, Florida 32611-7200, USA. katritzky@chem.ufl.edu alt-title: The Journal of organic chemistry number: 1 accession-num: 21158395
Keywords: Peptides/*chemistry; Molecular Structure; Cysteine/*chemistry; Acylation; Substrate Specificity; Sulfur/chemistry; Magnetic Resonance Spectroscopy; Peptides, Cyclic/*chemistry; Hydroxides/chemistry; Microwaves; Triazoles/*chemistry

N-methyl-phenacyloxycarbamidomethyl (Pocam) group: a novel thiol protecting group for solid-phase peptide synthesis and peptide condensation reactions - Katayama, H.; Nakahara, Y.; Hojo, H. (Org. Biomol. Chem., 2011)
In the so-called thioester method for the condensation of peptide segments, protecting groups for amino and thiol groups are required for chemoselective ligation. In this study, we developed a novel thiol protecting group, N-methyl-phenacyloxycarbamidomethyl (Pocam). We used it for protection of cysteine side chains, and synthesized Pocam-containing peptides and peptide thioesters. These were condensed by the thioester method. After the condensation reaction, Pocam groups were cleaved by Zn/AcOH treatment. At the same time, the azido group, which was used for the protection of lysine side chains, was also converted to an amino group, demonstrating that this protecting group strategy simplified the deprotecting reaction after the peptide condensation reaction to only one step.
Journal Article Research Support, Non-U.S. Gov't England
The following values have no corresponding Zotero field: auth-address: Department of Applied Biochemistry, Faculty of Engineering, Tokai University, Hiratsuka, Kanagawa 259-1292, Japan. katay@tokai-u.jp alt-title: Organic & biomolecular chemistry number: 12 accession-num: 21537511
Keywords: Animals; Humans; Solid-Phase Synthesis Techniques/*methods; Cysteine/*chemistry; Azides/chemistry; Chromatography, Reverse-Phase; Lysine/*chemistry; Chemistry, Pharmaceutical/*methods; Indicators and Reagents/*chemical synthesis; Peptides/analysis/*chemical synthesis; Zinc/chemistry

Site-specific introduction of an acetyl-lysine mimic into peptides and proteins by cysteine alkylation - Huang, Rong; Holbert, Marc A.; Tarrant, Mary Katherine; Curtet, Sandrine; Colquhoun, David R.; Dancy, Beverley M.; Dancy, Blair C.; Hwang, Yousang; Tang, Yong; Meeth, Katrina; Marmorstein, Ronen; Cole, Robert N.; et al. (J. Am. Chem. Soc., 2011)
Protein acetylation on Lys residues is recognized as a significant post-translational modification in cells, but it is often difficult to discern the direct structural and functional effects of individual acetylation events. Here we describe a new tool, methylthiocarbonyl-aziridine, to install acetyl-Lys mimics site-specifically into peptides and proteins by alkylation of Cys residues. We demonstrate that the resultant thiocarbamate modification can be recognized by the Brdt bromodomain and site-specific anti-acetyl-Lys antibodies, is resistant to histone deacetylase cleavage, and can confer activation of the histone acetyltransferase Rtt109 by simulating autoacetylation. We also use this approach to obtain functional evidence that acetylation of CK2 protein kinase on Lys102 can stimulate its catalytic activity.
0002-7863 1520-5126 20608637[pmid] J Am Chem Soc
The following values have no corresponding Zotero field: number: 29

Peptidyl N,N-bis(2-mercaptoethyl)-amides as thioester precursors for native chemical ligation - Hou, W.; Zhang, X.; Li, F.; Liu, C. F. (Org. Lett., 2011)
With two beta-mercaptoethyl groups on the N, a tertiary amide of structure 1 is always poised for intramolecular thioesterification however it flips about the C-N bond. It is shown that a peptide with such a C-terminal N,N-bis(2-mercaptoethyl)-amide (BMEA) can be used directly for native chemical ligation (NCL). These BMEA peptides are easily prepared with standard Fmoc-solid phase peptide synthesis protocols, thus giving a very convenient access to the thioester components for NCL.
1523-7052 (Electronic) 1523-7052 (Linking) Journal article
The following values have no corresponding Zotero field: auth-address: Division of Chemical Biology and Biotechnology, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551. accession-num: 21175148

Towards elucidation of the role of ubiquitination in the pathogenesis of Parkinson's disease with semisynthetic ubiquitinated alpha-synuclein - Hejjaoui, M.; Haj-Yahya, M.; Kumar, K. S.; Brik, A.; Lashuel, H. A. (Angew. Chem. Int. Ed., 2011)
1521-3773 (Electronic) 1433-7851 (Linking) Journal Article Research Support, Non-U.S. Gov't
The following values have no corresponding Zotero field: auth-address: Brain Mind Institute, The Swiss Federal Institute of Technology EPFL, Station 19, 1015 Lausanne, Switzerland. number: 2 accession-num: 21154793
Keywords: Amino Acid Sequence; Humans; Protein Binding; Molecular Sequence Data; Chromatography, High Pressure Liquid; Mass Spectrometry; alpha-Synuclein/chemical synthesis/*chemistry/metabolism; Parkinson Disease/etiology/*metabolism; Ubiquitination/physiology

Microwave-assisted chemical ligation of S-acyl peptides containing non-terminal cysteine residues - Hansen, F. K.; Ha, K.; Todadze, E.; Lillicotch, A.; Frey, A.; Katritzky, A. R. (Org. Biomol. Chem., 2011)
An efficient approach for the synthesis of a series of S-acyl peptides containing internal cysteine residues has been developed and the chemical long-range ligation of these S-acyl peptides via 5-, 8-, 11- and 14-membered cyclic transition states has been investigated. Our results include the first examples of successful isopeptide ligations starting from S-acyl peptides containing non-terminal cysteine residues and indicate that the cyclic transition states studied in this present paper are decreasingly favored in the order of their sizes 5>>14>11>>8.
Journal Article Research Support, Non-U.S. Gov't England
The following values have no corresponding Zotero field: auth-address: Center for Heterocyclic Compounds, Department of Chemistry, University of Florida, Gainesville, FL 32611-7200, USA. alt-title: Organic & biomolecular chemistry number: 20 accession-num: 21879126
Keywords: Cysteine/chemistry; Molecular Structure; Acylation; Microwaves; Peptides/*chemical synthesis

Native chemical ligation of hydrolysis-resistant 3'-peptidyl-tRNA mimics - Geiermann, A. S.; Polacek, N.; Micura, R. (J. Am. Chem. Soc., 2011)
Hydrolysis-resistant 3'-peptidyl-RNA conjugates that mimic tRNA termini represent a remarkable synthetic challenge, particularly if they contain amino acids with complex side-chain functionalities, such as arginines. Here we demonstrate a novel approach that combines solid-phase synthesis and bioconjugation to obtain these derivatives with high efficiency and purity. The key step is native chemical ligation of 3'-cysteinyl-RNA fragments to highly soluble peptide thioesters. The so-prepared 3'-peptidyl-RNA conjugates relate to resistance peptides that can render the ribosome resistant to macrolide antibiotics by a yet unknown ribosomal translation mechanism.
Geiermann, Anna-Skrollan Polacek, Norbert Micura, Ronald J Am Chem Soc. 2011 Nov 30;133(47):19068-71. doi: 10.1021/ja209053b. Epub 2011 Nov 3.
The following values have no corresponding Zotero field: auth-address: Institute of Organic Chemistry and Center for Molecular Biosciences, University of Innsbruck, Austria. alt-title: Journal of the American Chemical Society number: 47 edition: 2011/11/05 accession-num: 22050598 work-type: Research Support, Non-U.S. Gov't
Keywords: Molecular Conformation; Hydrolysis; Molecular Mimicry; RNA, Transfer, Amino Acyl/*chemistry

Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction - Fierz, B.; Chatterjee, C.; McGinty, R. K.; Bar-Dagan, M.; Raleigh, D. P.; Muir, T. W. (Nat. Chem. Biol., 2011)
Regulation of chromatin structure involves histone posttranslational modifications that can modulate intrinsic properties of the chromatin fiber to change the chromatin state. We used chemically defined nucleosome arrays to demonstrate that H2B ubiquitylation (uH2B), a modification associated with transcription, interferes with chromatin compaction and leads to an open and biochemically accessible fiber conformation. Notably, these effects were specific for ubiquitin, as compaction of chromatin modified with a similar ubiquitin-sized protein, Hub1, was only weakly affected. Applying a fluorescence-based method, we found that uH2B acts through a mechanism distinct from H4 tail acetylation, a modification known to disrupt chromatin folding. Finally, incorporation of both uH2B and acetylated H4 resulted in synergistic inhibition of higher-order chromatin structure formation, possibly a result of their distinct modes of action.
1552-4469 (Electronic) 1552-4450 (Linking) Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.
The following values have no corresponding Zotero field: auth-address: Laboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, New York, USA. number: 2 accession-num: 21196936
Keywords: Protein Conformation; Ubiquitination; Fluorescence Resonance Energy Transfer; Chromatin/*metabolism; Histones/*metabolism

Protein chemical synthesis by ligation of peptide hydrazides - Fang, Ge-Min; Li, Yi-Ming; Shen, Fei; Huang, Yi-Chao; Li, Jia-Bin; Lin, Yun; Cui, Hong-Kui; Liu, Lei (Angew. Chem. Int. Ed., 2011)
1521-3773
The following values have no corresponding Zotero field: number: 33 publisher: WILEY-VCH Verlag
Keywords: native chemical ligation; protein chemical synthesis; proteins; peptide hydrazides; protein design

DNA-triggered synthesis and bioactivity of proapoptotic peptides - Erben, A.; Grossmann, T. N.; Seitz, O. (Angew. Chem. Int. Ed., 2011)
Erben, Anne Grossmann, Tom N Seitz, Oliver Germany International ed. in English Angew Chem Int Ed Engl. 2011 Mar 14;50(12):2828-32. doi: 10.1002/anie.201007103. Epub 2011 Feb 21.
The following values have no corresponding Zotero field: auth-address: Institut fur Chemie der Humboldt Universitat zu Berlin, Germany. number: 12 edition: 2011/03/10 accession-num: 21387498 work-type: Research Support, Non-U.S. Gov't
Keywords: Peptides/*chemistry; Apoptosis; Caspase 3/metabolism; Caspase 9/metabolism; DNA/*chemistry; Peptide Nucleic Acids/chemical synthesis/chemistry; X-Linked Inhibitor of Apoptosis Protein/antagonists & inhibitors/metabolism

DNA-instructed acyl transfer reactions for the synthesis of bioactive peptides - Erben, A.; Grossmann, T. N.; Seitz, O. (Bioorg. Med. Chem. Lett., 2011)
We present a method which allows for the translation of nucleic acid information into the output of molecules that interfere with disease-related protein-protein interactions. The method draws upon a nucleic acid-templated reaction, in which adjacent binding of reactive conjugates triggers the transfer of an aminoacyl or peptidyl group from a donating thioester-linked PNA-peptide hybrid to a peptide-PNA acceptor. We evaluated the influence of conjugate structures on reactivity and sequence specificity. The DNA-triggered peptide synthesis proceeded sequence specifically and showed catalytic turnover in template. The affinity of the formed peptide conjugates for the BIR3 domain of the X-linked inhibitor of apoptosis protein (XIAP) is discussed.
Erben, Anne Grossmann, Tom N Seitz, Oliver England Bioorg Med Chem Lett. 2011 Sep 1;21(17):4993-7. doi: 10.1016/j.bmcl.2011.05.027. Epub 2011 May 14.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Humboldt-Universitat zu Berlin, Berlin 12489, Germany. alt-title: Bioorganic & medicinal chemistry letters number: 17 edition: 2011/06/15 accession-num: 21664815 work-type: Research Support, Non-U.S. Gov't
Keywords: Humans; Cell Line; Catalysis; Peptides/*chemical synthesis; DNA/*chemistry; Peptide Nucleic Acids/chemistry

Three-component synthesis of neoglycopeptides using a Cu(II)-triggered aminolysis of peptide hydrazide resin and an azide-alkyne cycloaddition sequence - Ebran, J. P.; Dendane, N.; Melnyk, O. (Org Lett, 2011)
Copper(II)-induced oxidative aminolysis of hydrazides generates Cu(I), the catalyst of the azide-alkyne cycloaddition. This feature was exploited to design a novel solid phase detaching three-component reaction permitting the conversion of supported peptide hydrazides into 1,2,3-triazole linked C-terminal neoglycopeptides.
Ebran, Jean-Philippe Dendane, Nabil Melnyk, Oleg Research Support, Non-U.S. Gov't United States Organic letters Org Lett. 2011 Aug 19;13(16):4336-9. doi: 10.1021/ol201659x. Epub 2011 Jul 18.
The following values have no corresponding Zotero field: auth-address: CNRS UMR 8161, Univ Lille Nord de France, Institut Pasteur de Lille, IFR 142 Molecular and Cellular Medicine, 1 rue du Pr Calmette 59021 Lille Cedex, France. number: 16 edition: 2011/07/20 accession-num: 21766830
Keywords: Peptides/*chemistry; Molecular Structure; Catalysis; Triazoles/chemistry; Oxidation-Reduction; Amines/*chemistry; Alkynes/*chemistry; Azides/*chemistry; Copper/*chemistry; Glycopeptides/*chemical synthesis

Preformed selenoesters enable rapid native chemical ligation at intractable sites - Durek, T.; Alewood, P. F. (Angew. Chem. Int. Ed., 2011)
1521-3773 (Electronic) 1433-7851 (Linking) Journal Article Research Support, Non-U.S. Gov't
The following values have no corresponding Zotero field: auth-address: Institute for Molecular Bioscience, The University of Queensland, 306 Carmody Rd, St Lucia, Brisbane, Australia. t.durek@uq.edu.au number: 50 accession-num: 21997950

Toward homogeneous erythropoietin: Application of metal-free dethiylation in the chemical synthesis of the Ala79-Arg166 glycopeptide domain - Dong, Suwei; Shang, Shiying; Tan, Zhongping; Danishefsky, Samuel J. (Isr. J. Chem., 2011)
1869-5868
The following values have no corresponding Zotero field: number: 8-9 publisher: WILEY-VCH Verlag
Keywords: ligation; total synthesis; glycoproteins; dethiylation; erythropoietin

Dual kinetically controlled native chemical ligation using a combination of sulfanylproline and sulfanylethylanilide peptide - Ding, H.; Shigenaga, A.; Sato, K.; Morishita, K.; Otaka, A. (Org. Lett., 2011)
Dual kinetically controlled native chemical ligation using a newly developed sulfanylproline-mediated reaction in combination with an N-sulfanylethylanilide peptide was successfully applied to a previously unreported sequential coupling of peptide fragments added simultaneously to the reaction.
1523-7052 (Electronic) 1523-7052 (Linking) Journal Article Research Support, Non-U.S. Gov't
The following values have no corresponding Zotero field: auth-address: Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima, Shomachi, Tokushima 770-8505, Japan. number: 20 accession-num: 21916452
Keywords: Amino Acid Sequence; Stereoisomerism; Kinetics; Molecular Structure; Peptides/chemical synthesis/*chemistry; Neuropeptides/chemical synthesis/*chemistry; Sulfhydryl Compounds/chemical synthesis/*chemistry

Synthesis of peptide alkylthioesters using the intramolecular N,S-acyl shift properties of bis(2-sulfanylethyl)amido peptides - Dheur, J.; Ollivier, N.; Vallin, A.; Melnyk, O. (J. Org. Chem., 2011)
The design of novel methods giving access to peptide alkylthioesters, the key building blocks for protein synthesis using Native Chemical Ligation, is an important area of research. Bis(2-sulfanylethyl)amido peptides (SEA peptides) 1 equilibrate in aqueous solution with S-2-(2-mercaptoethylamino)ethyl thioester peptides 2 through an N,S-acyl shift mechanism. HPLC was used to study the rate of equilibration for different C-terminal amino acids and the position of equilibrium as a function of pH. We show also that thioester form 2 can participate efficiently in a thiol-thioester exchange reaction with 5% aqueous 3-mercaptopropionic acid. The highest reaction rate was obtained at pH 4. These experimental conditions are significantly less acidic than those reported in the past for related systems. The method was validated with the synthesis of a 24-mer peptide thioester. Consequently, SEA peptides 1 constitute a powerful platform for access to native chemical ligation methodologies.
1520-6904 (Electronic) 0022-3263 (Linking) Journal article
The following values have no corresponding Zotero field: auth-address: CNRS UMR 8161, Universite Lille Nord de France, Institut Pasteur de Lille , IFR 142, 1 rue du Pr Calmette, 59021 Lille, France. number: 9 accession-num: 21417423

Synthesis of thiazolidine thioester peptides and acceleration of native chemical ligation - Dheur, J.; Ollivier, N.; Melnyk, O. (Org. Lett., 2011)
Thiazolidine thioester peptides were synthesized by reacting bis(2-sulfanylethyl)amido peptides with glyoxylic acid at pH 1. A significant increase in Native Chemical Ligation (NCL) rate was observed with thiazolidine thioesters compared to 3-mercaptopropionic acid-thioester analogues. The method is of particular interest for accelerating valine-cysteine peptide bond formation.
1523-7052 (Electronic) 1523-7052 (Linking) Journal Article
The following values have no corresponding Zotero field: auth-address: CNRS UMR 8161, Univ Lille Nord de France, Institut Pasteur de Lille, IFR 142 Molecular and Cellular Medicine, 1 rue du Pr Calmette 59021 Lille Cedex, France. number: 6 accession-num: 21348452

Surface PEGylation via native chemical ligation - Byun, Eunkyoung; Kim, Jangbae; Kang, Sung Min; Lee, Hyukjin; Bang, Duhee; Lee, Haeshin (Bioconjugate Chem., 2011)
The following values have no corresponding Zotero field: number: 1 publisher: American Chemical Society

Conformational preferences and pKa value of selenocysteine residue - Byun, B. J.; Kang, Y. K. (Biopolymers, 2011)
The conformational preferences of the L-selenocysteine (Sec) dipeptides with selenol and selenolate groups (Ac-Sec-NHMe and Ac-Sec(-) -NHMe, respectively) and the apparent (i.e., macroscopic) pK(a) value of the Sec residue have been studied using the dispersion-corrected density functionals M06-2X and B2PLYP-D with the implicit solvation method in the gas phase and in water. In the gas phase, the backbone-to-backbone and/or side chain-to-backbone hydrogen bonds are found to contribute in stabilizing the most preferred conformations for the Sec and Sec(-) residues, as seen for the Cys and Cys(-) residues. However, the polyproline II-like conformations prevail over the conformations with the backbone-to-backbone hydrogen bonds in water because of the weakened hydrogen bonds by the favorable direct interactions between the backbone CO and HN groups and water molecules. The Sec and Sec(-) residues are found to adopt more various conformations than the Cys and Cys(-) residues in water, although the most preferred conformations of the neutral and/or anionic forms of the two residues are similar each other in the gas phase and in water. Using the statistically weighted free energies of the Sec and Sec(-) dipeptides in the gas phase and their solvation free energies, the pK(a) value of the Sec residue is estimated to be 5.47 at 25 degrees C, which is in good agreement with the experimental value of 5.43 +/- 0.02. It is found that the lower pK(a) value of the selenol side chain for the Sec residue by approximately 3 units than the thiol side chain for the Cys residue is ascribed to the higher gas-phase acidity of the Sec residue.
Byun, Byung Jin Kang, Young Kee Biopolymers. 2011 May;95(5):345-53. doi: 10.1002/bip.21581. Epub 2011 Jan 6.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Chungbuk National University, Cheongju, Chungbuk 361-763, Republic of Korea. alt-title: Biopolymers number: 5 edition: 2011/01/08 accession-num: 21213257 work-type: Research Support, Non-U.S. Gov't
Keywords: Models, Molecular; Protein Conformation; Hydrogen-Ion Concentration; Hydrogen Bonding; Thermodynamics; Selenocysteine/*chemistry; Dipeptides/chemistry; Phase Transition; Selenoproteins/*chemistry; Solvents

The relative rates of thiol-thioester exchange and hydrolysis for alkyl and aryl thioalkanoates in water - Bracher, P. J.; Snyder, P. W.; Bohall, B. R.; Whitesides, G. M. (Orig. Life Evol. Biosph., 2011)
This article reports rate constants for thiol-thioester exchange (k (ex)), and for acid-mediated (k (a)), base-mediated (k (b)), and pH-independent (k (w)) hydrolysis of S-methyl thioacetate and S-phenyl 5-dimethylamino-5-oxo-thiopentanoate-model alkyl and aryl thioalkanoates, respectively-in water. Reactions such as thiol-thioester exchange or aminolysis could have generated molecular complexity on early Earth, but for thioesters to have played important roles in the origin of life, constructive reactions would have needed to compete effectively with hydrolysis under prebiotic conditions. Knowledge of the kinetics of competition between exchange and hydrolysis is also useful in the optimization of systems where exchange is used in applications such as self-assembly or reversible binding. For the alkyl thioester S-methyl thioacetate, which has been synthesized in simulated prebiotic hydrothermal vents, k (a) = 1.5 x 10(-5) M(-1) s(-1), k (b) = 1.6 x 10(-1) M(-1) s(-1), and k (w) = 3.6 x 10(-8) s(-1). At pH 7 and 23 degrees C, the half-life for hydrolysis is 155 days. The second-order rate constant for thiol-thioester exchange between S-methyl thioacetate and 2-sulfonatoethanethiolate is k (ex) = 1.7 M(-1) s(-1). At pH 7 and 23 degrees C, with [R''S(H)] = 1 mM, the half-life of the exchange reaction is 38 h. These results confirm that conditions (pH, temperature, pK (a) of the thiol) exist where prebiotically relevant thioesters can survive hydrolysis in water for long periods of time and rates of thiol-thioester exchange exceed those of hydrolysis by several orders of magnitude.
Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Netherlands the journal of the International Society for the Study of the Origin of Life
The following values have no corresponding Zotero field: auth-address: Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA. number: 5 accession-num: 21728078
Keywords: Temperature; Kinetics; Hydrogen-Ion Concentration; Sulfhydryl Compounds/*chemistry; *Organic Chemistry Processes; *Origin of Life; Acetates/chemistry; Alkanesulfonates/chemistry; Arylsulfonates/chemistry; Earth (Planet); Half-Life; Hydrothermal Vents/chemistry; Sulfides/*chemistry; Water/*chemistry

Chemical protein synthesis by kinetically controlled ligation of peptide O-esters - Zheng, J. S.; Cui, H. K.; Fang, G. M.; Xi, W. X.; Liu, L. (ChemBioChem, 2010)
1439-7633 (Electronic) 1439-4227 (Linking) Journal Article Research Support, Non-U.S. Gov't
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology, Tsinghua University, Beijing 100084, China. number: 4 accession-num: 20157912
Keywords: Amino Acid Sequence; Peptides/*chemical synthesis/chemistry; Molecular Sequence Data; Proteins/chemical synthesis/chemistry; Esters/*chemical synthesis; Sulfhydryl Compounds/*chemical synthesis

Synthesis of K48-linked diubiquitin using dual native chemical ligation at lysine - Yang, Renliang; Pasunooti, Kalyan Kumar; Li, Fupeng; Liu, Xue-Wei; Liu, Chuan-Fa (Chem. Commun., 2010)
The dual native chemical ligation at lysine strategy was revised by replacing the acid-labile Cbz protecting group with photolabile NVOC at the 4-mercaptolysine side chain. The optimized strategy was subsequently applied to the synthesis of K48-linked diubiquitin.
10.1039/C0CC01382J
The following values have no corresponding Zotero field: number: 38 publisher: The Royal Society of Chemistry

Promising general solution to the problem of ligating peptides and glycopeptides - Wang, P.; Danishefsky, S. J. (J Am Chem Soc, 2010)
Our global goal is that of synthesizing complex polypeptides and glycopeptides in homogeneous form. Chemistry-derived access to homogeneous biologics could well have useful consequences in the discovery of drugs and vaccines. The key finding in this study is that thio acids can become highly competent acyl donors following even trace levels of oxidative activation, thereby undergoing amide bond formation upon reaction with N-terminal peptides. Though our data set does not establish the specific mechanism of this reaction, a framework to account for the fact that minute levels of oxidation actuate amide bond formation with high turnover is offered. An apparently general coupling of thio acids (including complex peptide thio acids with N-termini of complex peptides) has thus been realized. These ligations are conducted with minimal alpha-epimerization in the C-terminal group and allow for the coupling of N-terminal and C-terminal glycopeptides en route to homogeneous glycoproteins.
The following values have no corresponding Zotero field: auth-address: Laboratory for Bioorganic Chemistry, Sloan-Kettering Institute for Cancer Research, 1275 York Avenue, New York, New York 10065, USA. number: 47 edition: 2010/11/06 accession-num: 21049949
Wang, Ping Danishefsky, Samuel J CA103823/CA/NCI NIH HHS/United States R01 CA103823-33/CA/NCI NIH HHS/United States R37 CA028824-33/CA/NCI NIH HHS/United States Research Support, N.I.H., Extramural United States Journal of the American Chemical Society J Am Chem Soc. 2010 Dec 1;132(47):17045-51. doi: 10.1021/ja1084628. Epub 2010 Nov 4.
Keywords: Amino Acid Sequence; Molecular Sequence Data; Triazoles/chemistry; Glycopeptides/chemical synthesis/*chemistry

Alternative chemistries for the synthesis of thrombospondin-1 type 1 repeats - Tiefenbrunn, T. K.; Blanco-Canosa, J.; Dawson, P. E. (Biopolymers, 2010)
Synthetic protein engineering has benefited from the development of diverse methods for the synthesis of functionalized peptide fragments and approaches for their subsequent assembly into full length polypeptides. Here we describe a series of synthetic approaches for the total chemical synthesis of the second type 1 repeat of thrombospondin-1 (TSR2) that vary in both the location of the ligation site and alpha-amine protecting group strategy (Boc/Fmoc) used for the synthesis of the associated peptide fragments. These syntheses illustrate that challenging peptide sequences can result from the protecting group strategy as well as from sequence-dependent factors. Importantly, we find that such challenges can be overcome by altering the chemistry used for solid phase peptide synthesis, the choice of ligation site, and the resin used as a solid support. From these studies, we have developed a robust synthetic route to the TSR2 polypeptide consisting of native chemical ligation between an N-terminal fragment synthesized by Boc-SPPS and a C-terminal fragment synthesized by Fmoc-SPPS. Finally, the folded TSR2 domain is obtained following an optimized oxidative folding protocol using an excess of oxidized glutathione. This optimized synthesis will enable the use of unnatural amino acids to probe the unusual structure and anti-angiogenic activity of this protein domain.
R01 GM059380/GM/NIGMS NIH HHS/United States R01 GM059380-09/GM/NIGMS NIH HHS/United States Journal Article United States
The following values have no corresponding Zotero field: auth-address: Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. alt-title: Biopolymers number: 4 accession-num: 20593462
Keywords: Humans; Peptides/*chemical synthesis/chemistry; Amino Acid Motifs; Thrombospondin 1/*chemical synthesis/chemistry

A reasonably stereospecific multistep conversion of Boc-protected a-amino acids to Phth-protected b3-amino acids - Temperini, Andrea; Capperucci, Antonella; Degl'Innocenti, Alessandro; Terlizzi, Raffaella; Tiecco, Marcello (Tetrahedron Lett., 2010)
A method for the synthesis of β3-amino acids starting from α-amino acids is described. This conversion can be effected by an eight-step procedure which involves the transformation of the carboxylic group into an alkyne followed by a selenium-mediated conversion of the carbon–carbon triple bond to a Se-phenyl selenocarboxylate intermediate. The reactive Se-phenyl selenocarboxylate intermediates can be trapped with water, alcohols or the amine of an amino acid derivative to give β3-amino acids, β3-amino esters or mixed peptides, respectively. The whole transformations of the carboxylic group into an alkyne and of the alkyne group into β3-amino acids may not require purification of the intermediate products but a work-up and isolation procedure of crude materials.
0040-4039
The following values have no corresponding Zotero field: number: 31
Keywords: Î±-Amino acids; Î²-Amino acids; Propargylic amines; Selenium

Insights into the finer issues of native chemical ligation: An approach to cascade ligations - Tan, Zhongping; Shang, Shiying; Danishefsky, Samuel J. (Angew. Chem. Int. Ed., 2010)
1521-3773
The following values have no corresponding Zotero field: number: 49 publisher: WILEY-VCH Verlag
Keywords: native chemical ligation; peptides; desulfurization; kinetic control; leucine

Design and folding of [GluA4(ObetaThrB30)]insulin ("ester insulin"): a minimal proinsulin surrogate that can be chemically converted into human insulin - Sohma, Y.; Hua, Q. X.; Whittaker, J.; Weiss, M. A.; Kent, S. B. H. (Angew. Chem. Int. Ed., 2010)
R01 GM075993/GM/NIGMS NIH HHS/United States R01 GM075993-01/GM/NIGMS NIH HHS/United States DK040949/DK/NIDDK NIH HHS/United States DK074176/DK/NIDDK NIH HHS/United States Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Germany
The following values have no corresponding Zotero field: auth-address: Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637, USA. ysohma@mb.kyoto-phu.ac.jp alt-title: Angewandte Chemie (International ed number: 32 accession-num: 20509131
Keywords: Amino Acid Sequence; Humans; Molecular Sequence Data; Protein Folding; Disulfides/chemistry; Insulin/chemistry; Proinsulin/chemical synthesis/*chemistry

Nonhydrolyzable ubiquitin-isopeptide isosteres as deubiquitinating enzyme probes - Shanmugham, A.; Fish, A.; Luna-Vargas, M. P.; Faesen, A. C.; El Oualid, F.; Sixma, T. K.; Ovaa, H. (J. Am. Chem. Soc., 2010)
We demonstrate that oxime ligation is an efficient, straightforward, and generally applicable strategy for generating nonhydrolyzable ubiquitin (Ub)-isopeptide isosteres. We synthesized nonhydrolyzable K48- and K63-linked Ub-isopeptide isosteres to investigate the selectivity of deubiquitinating enzymes for specific linkages employing surface plasmon resonance spectroscopy. The results indicate that deubiquitinating enzymes specifically recognize the local peptide sequence flanking Ub-branched lysine residues in target proteins. The described strategy allows the systematic investigation of sequence requirements for substrate selectivity of deubiquitinating enzymes.
Shanmugham, Anitha Fish, Alexander Luna-Vargas, Mark P A Faesen, Alex C El Oualid, Farid Sixma, Titia K Ovaa, Huib Research Support, Non-U.S. Gov't United States Journal of the American Chemical Society J Am Chem Soc. 2010 Jul 7;132(26):8834-5. doi: 10.1021/ja101803s.
The following values have no corresponding Zotero field: auth-address: Division of Cell Biology and The Netherlands Proteomics Centre, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands. number: 26 edition: 2010/06/15 accession-num: 20540574
Keywords: Amino Acid Sequence; Models, Molecular; Protein Conformation; Molecular Sequence Data; Substrate Specificity; Endopeptidases/*metabolism; Biosensing Techniques/*methods; Peptides/chemistry/*metabolism; Ubiquitin/chemistry/*metabolism

Cyclic peptide synthesis with thioacids - Sasaki, Kaname; Crich, David (Org. Lett., 2013)
doi: 10.1021/ol101201w
The following values have no corresponding Zotero field: number: 14 publisher: American Chemical Society

Ligation-desulfurization: a powerful combination in the synthesis of peptides and glycopeptides - Rohde, H.; Seitz, O. (Biopolymers, 2010)
The native chemical ligation enables the chemoselective coupling of two unprotected protein segments. In the initial format of this reaction, the side chain of N-terminal cysteine residues serves to capture a peptide thioester. The N-terminus of the cysteinyl peptide is involved in a subsequent intramolecular aminolysis reaction, upon which the "native" peptide bond is established. Considerable efforts have been invested to remove the restriction to cysteine-containing ligation sites. In this review, we focus on the combination of two chemoselective reactions, native chemical ligation, and desulfurization, which has extended the repertoire of accessible ligation junctions. Based on this two-step approach, native alanine-containing peptides are accessible through postligation desulfurization of cysteine-ligation products. Recently, significant progress has been achieved in the development of new thiolated building blocks that serve as precursors to other amino acids. Ligations at phenylalanine can be accomplished by means of a beta-mercaptophenylalanine building block and subsequent desulfurization. The building blocks beta-mercaptovaline (penicillamine) and gamma-mercaptovaline provide access to hydrophobic ligation sites (Xaa-Val). Lysine has been equipped with a delta- and gamma-mercapto groups, which enables ligations at both the alpha- and the epsilon-amino group. This review also describes the recent improvements of desulfurization chemistry, which have widened the scope of the ligation-desulfurization approach and offer a promising alternative for the synthesis of Cys-free peptides and glycopeptides.
0006-3525 (Print) 0006-3525 (Linking) Journal Article Review
The following values have no corresponding Zotero field: auth-address: Institute of Chemistry, Humboldt-University of Berlin, Brook-Taylor-Str. 2, 12489 Berlin, Germany. number: 4 accession-num: 20593472
Keywords: Sulfhydryl Compounds/*chemistry; Glycopeptides/*chemical synthesis/*chemistry; Phenylalanine/chemistry

Detection and analysis of chimeric tertiary structures by backbone thioester exchange: packing of an alpha helix against an alpha/beta-peptide helix - Price, J. L.; Hadley, E. B.; Steinkruger, J. D.; Gellman, S. H. (Angew. Chem. Int. Ed., 2010)
Price, Joshua L Hadley, Erik B Steinkruger, Jay D Gellman, Samuel H GM-61238/GM/NIGMS NIH HHS/United States R01 GM061238-01/GM/NIGMS NIH HHS/United States R01 GM061238-02/GM/NIGMS NIH HHS/United States R01 GM061238-03/GM/NIGMS NIH HHS/United States R01 GM061238-04/GM/NIGMS NIH HHS/United States R01 GM061238-05/GM/NIGMS NIH HHS/United States R01 GM061238-06/GM/NIGMS NIH HHS/United States R01 GM061238-07/GM/NIGMS NIH HHS/United States R01 GM061238-08/GM/NIGMS NIH HHS/United States R01 GM061238-09/GM/NIGMS NIH HHS/United States R01 GM061238-10/GM/NIGMS NIH HHS/United States R01 GM061238-10S1/GM/NIGMS NIH HHS/United States T32 GM008505/GM/NIGMS NIH HHS/United States Research Support, N.I.H., Extramural Germany Angewandte Chemie (International ed. in English) Angew Chem Int Ed Engl. 2010;49(2):368-71. doi: 10.1002/anie.200904714.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706, USA. number: 2 edition: 2009/12/08 accession-num: 19967682
Keywords: Computational Biology; Protein Conformation; Hydrogen-Ion Concentration; Esters/chemistry; Peptides/*chemical synthesis/chemistry; Chromatography, High Pressure Liquid; Amino Acids/chemistry; Thermodynamics; Protein Folding; Structure-Activity Relationship; Sulfhydryl Compounds/chemistry; Protein Structure, Secondary; Helix-Loop-Helix Motifs; Mutant Chimeric Proteins/chemical synthesis/*chemistry; Ultracentrifugation

A highly unusual thioester bond in a pilus adhesin is required for efficient host cell interaction - Pointon, J. A.; Smith, W. D.; Saalbach, G.; Crow, A.; Kehoe, M. A.; Banfield, M. J. (J. Biol. Chem., 2010)
Many bacterial pathogens present adhesins at the tips of long macromolecular filaments known as pili that are often important virulence determinants. Very little is known about how pili presented by Gram-positive pathogens mediate host cell binding. The crystal structure of a pilus adhesin from the important human pathogen Streptococcus pyogenes reveals an internal thioester bond formed between the side chains of a cysteine and a glutamine residue. The presence of the thioester was verified using UV-visible spectroscopy and mass spectrometry. This unusual bond has only previously been observed in thioester domains of complement and complement-like proteins where it is used to form covalent attachment to target molecules. The structure also reveals two intramolecular isopeptide bonds, one of these formed through a Lys/Asp residue pair, which are strategically positioned to confer protein stability. Removal of the internal thioester by allele-replacement mutagenesis in S. pyogenes severely compromises bacterial adhesion to model host cells. Although current paradigms of bacterial/host cell interaction envisage strong non-covalent interactions, the present study suggests cell adhesion could also involve covalent bonds.
G0400849/Medical Research Council/United Kingdom G0500367/Medical Research Council/United Kingdom G0600309/Medical Research Council/United Kingdom Journal Article Research Support, Non-U.S. Gov't United States
The following values have no corresponding Zotero field: auth-address: Institute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, United Kingdom. alt-title: The Journal of biological chemistry number: 44 accession-num: 20729215
Keywords: Escherichia coli/metabolism; Protein Binding; Peptides/chemistry; Crystallography, X-Ray/methods; Esters/*chemistry; Adhesins, Bacterial/*chemistry; Alleles; Aspartic Acid/chemistry; Cell Adhesion; Fimbriae, Bacterial/*metabolism; Lysine/chemistry; Mutagenesis; Spectrophotometry, Ultraviolet/methods; Streptococcus pneumoniae/metabolism; Streptococcus pyogenes/*metabolism

Total chemical synthesis and X-ray structure of kaliotoxin by racemic protein crystallography - Pentelute, B. L.; Mandal, K.; Gates, Z. P.; Sawaya, M. R.; Yeates, T. O.; Kent, S. B. H. (Chem. Commun., 2010)
Here we report the total synthesis of kaliotoxin by 'one pot' native chemical ligation of three synthetic peptides. A racemic mixture of D- and L-kaliotoxin synthetic protein molecules gave crystals in the centrosymmetric space group P1 that diffracted to atomic-resolution (0.95 A), enabling the X-ray structure of kaliotoxin to be determined by direct methods.
1364-548X (Electronic) 1359-7345 (Linking) Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.
The following values have no corresponding Zotero field: auth-address: Department of Chemistry, Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois 60637, USA. number: 43 accession-num: 20877851
Keywords: Amino Acid Sequence; Stereoisomerism; Molecular Sequence Data; Peptides/chemical synthesis/chemistry; Crystallography, X-Ray; Protein Structure, Tertiary; Scorpion Venoms/*chemical synthesis/chemistry

Bis(2-sulfanylethyl)amino native peptide ligation - Ollivier, N.; Dheur, J.; Mhidia, R.; Blanpain, A.; Melnyk, O. (Org. Lett., 2010)
The reaction of a peptide featuring a bis(2-sulfanylethyl)amino (SEA) group on its C-terminus with a cysteinyl peptide in water at pH 7 and 37 degrees C leads to the chemoselective and regioselective formation of a native peptide bond. This method called SEA ligation enriches the native peptide ligation repertoire available to the peptide chemist. Preparation of an innovative solid support which allows the straightforward synthesis of peptide SEA fragments using standard Fmoc/tert-butyl solid phase peptide synthesis procedures is also described.
1523-7052 (Electronic) 1523-7052 (Linking) Journal Article Research Support, Non-U.S. Gov't
The following values have no corresponding Zotero field: auth-address: CNRS UMR 8161, Univ Lille Nord de France, Institut Pasteur de Lille, IFR 142 Molecular and Cellular Medicine, 1 rue du Pr Calmette 59021 Lille Cedex, France. number: 22 accession-num: 20964289
Keywords: Stereoisomerism; Molecular Structure; Peptides/*chemical synthesis/chemistry; Sulfhydryl Compounds/*chemical synthesis/chemistry

High-pressure-promoted Fmoc-aminoacylation of N-ethylcysteine: preparation of key devices for the solid-phase synthesis of peptide thioesters - Nakahara, Yuko; Matsuo, Ichiro; Ito, Yukishige; Ubagai, Risa; Hojo, Hironobu; Nakahara, Yoshiaki (Tetrahedron Lett., 2010)
In this study synthesis of Fmoc-aminoacyl-N-ethyl-S-triphenylmethylcysteine, a new Nâ†’S acyl migratory device for the preparation of peptide thioesters by Fmoc solid-phase peptide synthesis (SPPS) is described. Condensation of Fmoc-aminoacyl fluoride and N-ethyl-S-triphenylmethylcysteine allyl ester, readily prepared from known S-triphenylmethylcysteine allyl ester, was efficiently promoted in CH2Cl2 under high-pressure (800 MPa). When the reaction was performed with the additive DIEA, considerable epimerization at the chiral centers occurred, affording a mixture of diastereomers. When the preparation procedure for N-ethyl-S-triphenylmethylcysteine allyl ester was changed and the additive DIEA in the high-pressure reaction was excluded, Fmoc-aminoacyl-N-ethyl-S-triphenylmethylcysteines was obtained as a single stereoisomer without epimerization. The Fmoc-l-leucine adduct thus prepared was deallylated and used for the SPPS of a known decapeptide. A remarkable increase (44%) in the overall yield of the decapeptidethioester was achieved, compared to the 7% obtained by the stepwise on-resin Leu-Cys condensation method.
0040-4039
The following values have no corresponding Zotero field: number: 2

Synthesis of the glycosylated polypeptide chain of an inducible costimulator on T-cells - Murase, T.; Kajihara, Y. (Carbohydr. Res., 2010)
The glycoprotein AILIM/ICOS (Activation inducible lymphocyte immunomediately molecule/Inducible co-stimulator) on T-cells was identified in 1998 as a member of the CD28/CTLA4 family. The three-dimensional structure of the AILIM/ICOS extracellular domain has not been solved, and therefore we have examined the preparation of homogeneous glycosylated polypeptide chains of this domain having two homogeneous N-linked complex type oligosaccharides for use in folding experiments. To synthesize the glycosylated whole polypeptide chain of the AILIM/ICOS extracellular domain, the target polypeptide chain was divided into four segments, each containing a cysteine residue. Those peptide segments were synthesized by conventional SPPS, followed by thioesterification of the C-terminus. The oligosaccharide moiety, a biantennary complex type disialyloligosaccharide, was attached to the cysteine thiol in the peptide backbone using the haloacetamide method. These peptides, as well as a glycosylated peptide, were sequentially coupled by use of native chemical ligation. This process successfully afforded the desired polypeptide chain having homogeneous oligosaccharides.
Journal Article Research Support, Non-U.S. Gov't Netherlands
The following values have no corresponding Zotero field: auth-address: International Graduate School of Arts and Sciences, Yokohama City University, 22-2, Seto, Kanazawa-ku, Yokohama, Kanagawa 236-0027, Japan. alt-title: Carbohydrate research number: 10 accession-num: 20362277
Keywords: Amino Acid Sequence; Molecular Sequence Data; Chromatography, High Pressure Liquid; Mass Spectrometry; Glycosylation; Protein Folding; Peptides/*chemical synthesis/*chemistry; Antigens, Differentiation, T-Lymphocyte/*chemistry; Inducible T-Cell Co-Stimulator Protein