Synthesis of β-Thiol Phenylalanine for Applications in One-Pot Ligation–Desulfurization Chemistry - Malins, Lara R.; Giltrap, Andrew M.; Dowman, Luke J.; Payne, Richard J. (Organic Letters, 2015)

Rapid assembly and profiling of an anticoagulant sulfoprotein library - Watson, Emma E.; Ripoll-Rozada, Jorge; Lee, Ashley C.; Wu, Mike C. L.; Franck, Charlotte; Pasch, Tim; Premdjee, Bhavesh; Sayers, Jessica; Pinto, Maria F.; Martins, Pedro M.; Jackson, Shaun P.; Pereira, Pedro José Barbosa; et al. (Proceedings of the National Academy of Sciences, 2019)
Hematophagous organisms produce a suite of salivary proteins which interact with the host’s coagulation machinery to facilitate the acquisition and digestion of a bloodmeal. Many of these biomolecules inhibit the central blood-clotting serine proteinase thrombin that is also the target of several clinically approved anticoagulants. Here a bioinformatics approach is used to identify seven tick proteins with putative thrombin inhibitory activity that we predict to be posttranslationally sulfated at two conserved tyrosine residues. To corroborate the biological role of these molecules and investigate the effects of amino acid sequence and sulfation modifications on thrombin inhibition and anticoagulant activity, a library of 34 homogeneously sulfated protein variants were rapidly assembled using one-pot diselenide-selenoester ligation (DSL)-deselenization chemistry. Downstream functional characterization validated the thrombin-directed activity of all target molecules and revealed that posttranslational sulfation of specific tyrosine residues crucially modulates potency. Importantly, access to this homogeneously modified protein library not only enabled the determination of key structure–activity relationships and the identification of potent anticoagulant leads, but also revealed subtleties in the mechanism of thrombin inhibition, between and within the families, that would be impossible to predict from the amino acid sequence alone. The synthetic platform described here therefore serves as a highly valuable tool for the generation and thorough characterization of libraries of related peptide and/or protein molecules (with or without modifications) for the identification of lead candidates for medicinal chemistry programs.

Alternative chemistries for the synthesis of thrombospondin-1 type 1 repeats - Tiefenbrunn, Theresa K.; Blanco-Canosa, Juan; Dawson, Philip E. (Biopolymers, 2010)

Alternative chemistries for the synthesis of thrombospondin-1 type 1 repeats - Tiefenbrunn, Theresa K.; Blanco-Canosa, Juan; Dawson, Philip E. (Biopolymers, 2010)

Efficient peptide ligation between allyl-protected Asp and Cys followed by palladium-mediated deprotection - Kamo, Naoki; Hayashi, Gosuke; Okamoto, Akimitsu (Chemical Communications, 2018)
Difficult peptide ligation between Asp and Cys and subsequent deprotection proceeded in one pot by adding a small amount of Pd/TPPTS complex. , An efficient method for peptide ligation between C-terminal Asp(OAllyl) and N-terminal Cys has been developed. Peptide ligation and removal of the allyl group at the Asp carboxylate side chain proceeded in one pot by adding a small amount of Pd/TPPTS complex. Based on this efficient synthetic method, PEP-19 (61 amino acids), which is highly expressed in Purkinje cells, was synthesized.

Chemical synthesis of transactivation domain (TAD) of tumor suppressor protein p53 by native chemical ligation of three peptide segments - Baral, Abhishek; Asokan, Aromal; Bauer, Valentin; Kieffer, Bruno; Torbeev, Vladimir (Tetrahedron, 2019)

Efficient peptide ligation between allyl-protected Asp and Cys followed by palladium-mediated deprotection - Kamo, Naoki; Hayashi, Gosuke; Okamoto, Akimitsu (Chemical Communications, 2018)
Difficult peptide ligation between Asp and Cys and subsequent deprotection proceeded in one pot by adding a small amount of Pd/TPPTS complex. , An efficient method for peptide ligation between C-terminal Asp(OAllyl) and N-terminal Cys has been developed. Peptide ligation and removal of the allyl group at the Asp carboxylate side chain proceeded in one pot by adding a small amount of Pd/TPPTS complex. Based on this efficient synthetic method, PEP-19 (61 amino acids), which is highly expressed in Purkinje cells, was synthesized.

Chemical synthesis of transactivation domain (TAD) of tumor suppressor protein p53 by native chemical ligation of three peptide segments - Baral, Abhishek; Asokan, Aromal; Bauer, Valentin; Kieffer, Bruno; Torbeev, Vladimir (Tetrahedron, 2019)

Total Synthesis of Human Galanin-Like Peptide through an Aspartic Acid Ligation - Guan, Xiaoyang; Drake, Matthew R.; Tan, Zhongping (Organic Letters, 2013)

Total Synthesis of Human Galanin-Like Peptide through an Aspartic Acid Ligation - Guan, Xiaoyang; Drake, Matthew R.; Tan, Zhongping (Organic Letters, 2013)

Peptide Ligation-Desulfurization Chemistry at Arginine - Malins, Lara R.; Cergol, Katie M.; Payne, Richard J. (ChemBioChem, 2013)

Peptide Ligation-Desulfurization Chemistry at Arginine - Malins, Lara R.; Cergol, Katie M.; Payne, Richard J. (ChemBioChem, 2013)

Tyrosine sulfation modulates activity of tick-derived thrombin inhibitors - Thompson, Robert E.; Liu, Xuyu; Ripoll-Rozada, Jorge; Alonso-García, Noelia; Parker, Benjamin L.; Pereira, Pedro José Barbosa; Payne, Richard J. (Nature Chemistry, 2017)

Tyrosine sulfation modulates activity of tick-derived thrombin inhibitors - Thompson, Robert E.; Liu, Xuyu; Ripoll-Rozada, Jorge; Alonso-García, Noelia; Parker, Benjamin L.; Pereira, Pedro José Barbosa; Payne, Richard J. (Nature Chemistry, 2017)

A device that operates within a self-assembled 3D DNA crystal - Hao, Yudong; Kristiansen, Martin; Sha, Ruojie; Birktoft, Jens J.; Hernandez, Carina; Mao, Chengde; Seeman, Nadrian C. (Nature Chemistry, 2017)

A device that operates within a self-assembled 3D DNA crystal - Hao, Yudong; Kristiansen, Martin; Sha, Ruojie; Birktoft, Jens J.; Hernandez, Carina; Mao, Chengde; Seeman, Nadrian C. (Nature Chemistry, 2017)

Chlorodifluoromethane-triggered formation of difluoromethylated arenes catalysed by palladium - Feng, Zhang; Min, Qiao-Qiao; Fu, Xia-Ping; An, Lun; Zhang, Xingang (Nature Chemistry, 2017)

Chlorodifluoromethane-triggered formation of difluoromethylated arenes catalysed by palladium - Feng, Zhang; Min, Qiao-Qiao; Fu, Xia-Ping; An, Lun; Zhang, Xingang (Nature Chemistry, 2017)

Racemic X-ray structure of L-type calcium channel antagonist Calciseptine prepared by total chemical synthesis - Chen, Chen-Chen; Gao, Shuai; Ai, Hua-Song; Qu, Qian; Tian, Chang-Lin; Li, Yi-Ming (Science China Chemistry, 2018)

Racemic X-ray structure of L-type calcium channel antagonist Calciseptine prepared by total chemical synthesis - Chen, Chen-Chen; Gao, Shuai; Ai, Hua-Song; Qu, Qian; Tian, Chang-Lin; Li, Yi-Ming (Science China Chemistry, 2018)

Direct synthesis of N-terminal thiazolidine-containing peptide thioesters from peptide hydrazides - Sato, Kohei; Tanaka, Shoko; Yamamoto, Kazuki; Tashiro, Yosuke; Narumi, Tetsuo; Mase, Nobuyuki (Chemical Communications, 2018)
We report a simple and promising synthetic method to oxidize peptide hydrazides containing N-terminal thiazolidine as a protected cysteine. , We report a simple and promising synthetic method to oxidize peptide hydrazides containing N-terminal thiazolidine as a protected cysteine. This yields the corresponding thioester via a peptide azide without decomposition of the thiazolidine ring. The newly developed protocol was validated by the synthesis of the bioactive peptide LacZα.

Direct synthesis of N-terminal thiazolidine-containing peptide thioesters from peptide hydrazides - Sato, Kohei; Tanaka, Shoko; Yamamoto, Kazuki; Tashiro, Yosuke; Narumi, Tetsuo; Mase, Nobuyuki (Chemical Communications, 2018)
We report a simple and promising synthetic method to oxidize peptide hydrazides containing N-terminal thiazolidine as a protected cysteine. , We report a simple and promising synthetic method to oxidize peptide hydrazides containing N-terminal thiazolidine as a protected cysteine. This yields the corresponding thioester via a peptide azide without decomposition of the thiazolidine ring. The newly developed protocol was validated by the synthesis of the bioactive peptide LacZα.

Acceleration of thiol additive-free native chemical ligation by intramolecular S → S acyl transfer - Schmalisch, J.; Seitz, O. (Chemical Communications, 2015)
The old dog and a new trick; mercaptopropionylcysteine (MPA–Cys) peptide thioesters show a surprisingly high reactivity in native chemical ligation (NCL) and allow thiol-additive free reactions. This facilitates sequential NCL reactions and ligation–desulfurization reactions in one-pot formats. The synthetic utility is demonstrated by the synthesis of a SH3 domain. , Peptide–mercaptopropionylcysteine (MPA–Cys) thioesters show a surprisingly high reactivity in native chemical ligation (NCL) and allow thiol-additive free reactions. This facilitates sequential NCL reactions and ligation–desulfurization reactions in one-pot formats. The synthetic utility is demonstrated by the synthesis of a SH3 domain.

Acceleration of thiol additive-free native chemical ligation by intramolecular S → S acyl transfer - Schmalisch, J.; Seitz, O. (Chemical Communications, 2015)
The old dog and a new trick; mercaptopropionylcysteine (MPA–Cys) peptide thioesters show a surprisingly high reactivity in native chemical ligation (NCL) and allow thiol-additive free reactions. This facilitates sequential NCL reactions and ligation–desulfurization reactions in one-pot formats. The synthetic utility is demonstrated by the synthesis of a SH3 domain. , Peptide–mercaptopropionylcysteine (MPA–Cys) thioesters show a surprisingly high reactivity in native chemical ligation (NCL) and allow thiol-additive free reactions. This facilitates sequential NCL reactions and ligation–desulfurization reactions in one-pot formats. The synthetic utility is demonstrated by the synthesis of a SH3 domain.

Synthesis of Disulfide Surrogate Peptides Incorporating Large‐Span Surrogate Bridges Through a Native‐Chemical‐Ligation‐Assisted Diaminodiacid Strategy - Qu, Qian; Gao, Shuai; Wu, Fangming; Zhang, Meng‐Ge; Li, Ying; Zhang, Long‐Hua; Bierer, Donald; Tian, Chang‐Lin; Zheng, Ji‐Shen; Liu, Lei (Angewandte Chemie International Edition, 2020)

Synthesis of Disulfide Surrogate Peptides Incorporating Large‐Span Surrogate Bridges Through a Native‐Chemical‐Ligation‐Assisted Diaminodiacid Strategy - Qu, Qian; Gao, Shuai; Wu, Fangming; Zhang, Meng‐Ge; Li, Ying; Zhang, Long‐Hua; Bierer, Donald; Tian, Chang‐Lin; Zheng, Ji‐Shen; Liu, Lei (Angewandte Chemie International Edition, 2020)

Solid-phase synthesis of peptide selenoesters via a side-chain anchoring strategy - Hanna, Cameron C.; Kulkarni, Sameer S.; Watson, Emma E.; Premdjee, Bhavesh; Payne, Richard J. (Chemical Communications, 2017)
A robust, high yielding and epimerisation-free solid-phase method for accessing peptide selenoesters is reported. , Peptide selenoesters have recently emerged as key building blocks for the ligation-based assembly of large polypeptides and proteins. Herein, we report an efficient solid-phase method for the high yielding and epimerisation-free synthesis of peptide selenoesters using a side-chain immobilisation strategy.

Solid-phase synthesis of peptide selenoesters via a side-chain anchoring strategy - Hanna, Cameron C.; Kulkarni, Sameer S.; Watson, Emma E.; Premdjee, Bhavesh; Payne, Richard J. (Chemical Communications, 2017)
A robust, high yielding and epimerisation-free solid-phase method for accessing peptide selenoesters is reported. , Peptide selenoesters have recently emerged as key building blocks for the ligation-based assembly of large polypeptides and proteins. Herein, we report an efficient solid-phase method for the high yielding and epimerisation-free synthesis of peptide selenoesters using a side-chain immobilisation strategy.

Chemical synthesis of a two-domain scorpion toxin LaIT2 and its single-domain analogs to elucidate structural factors important for insecticidal and antimicrobial activities - Juichi, Hironori; Ando, Ryo; Ishido, Takafumi; Miyashita, Masahiro; Nakagawa, Yoshiaki; Miyagawa, Hisashi (Journal of Peptide Science, 2018)

Synthetic Circularized Analogues of Bovine Pancreatic Trypsin Inhibitor - Tulla-Puche, Judit; Getun, IrinaV.; Alsina, Jordi; Albericio, Fernando; Barany, George (European Journal of Organic Chemistry, 2004)

A Native Chemical Ligation Approach for Combinatorial Assembly of Affibody Molecules - Lindgren, Joel; Ekblad, Caroline; Abrahmsén, Lars; Eriksson Karlström, Amelie (ChemBioChem, 2012)

Fluorine teams up with water to restore inhibitor activity to mutant BPTI - Ye, Shijie; Loll, Bernhard; Berger, Allison Ann; Mülow, Ulrike; Alings, Claudia; Wahl, Markus Christian; Koksch, Beate (Chemical Science, 2015)
Fluorinated derivatives of aminobutyric acid engage in unique interactions with structural waters within the BPTI/trypsin interface and restore inhibitor activity. , Introducing fluorine into molecules has a wide range of effects on their physicochemical properties, often desirable but in most cases unpredictable. The fluorine atom imparts the C–F bond with low polarizability and high polarity, and significantly affects the behavior of neighboring functional groups, in a covalent or noncovalent manner. Here, we report that fluorine, present in the form of a single fluoroalkyl amino acid side chain in the P1 position of the well-characterized serine-protease inhibitor BPTI, can fully restore inhibitor activity to a mutant that contains the corresponding hydrocarbon side chain at the same site. High resolution crystal structures were obtained for four BPTI variants in complex with bovine β-trypsin, revealing changes in the stoichiometry and dynamics of water molecules in the S1 subsite. These results demonstrate that the introduction of fluorine into a protein environment can result in “chemical complementation” that has a significantly favorable impact on protein–protein interactions.

Chemical synthesis of a two-domain scorpion toxin LaIT2 and its single-domain analogs to elucidate structural factors important for insecticidal and antimicrobial activities - Juichi, Hironori; Ando, Ryo; Ishido, Takafumi; Miyashita, Masahiro; Nakagawa, Yoshiaki; Miyagawa, Hisashi (Journal of Peptide Science, 2018)

Synthetic Circularized Analogues of Bovine Pancreatic Trypsin Inhibitor - Tulla-Puche, Judit; Getun, IrinaV.; Alsina, Jordi; Albericio, Fernando; Barany, George (European Journal of Organic Chemistry, 2004)

A Native Chemical Ligation Approach for Combinatorial Assembly of Affibody Molecules - Lindgren, Joel; Ekblad, Caroline; Abrahmsén, Lars; Eriksson Karlström, Amelie (ChemBioChem, 2012)

Synthetic Approaches to Disulfide-free Circular Bovine Pancreatic Trypsin Inhibitor (c-BPTI) Analogues - Tulla-Puche, Judit; Getun, Irina V.; Angell, Yvonne M.; Alsina, Jordi; Albericio, Fernando; Woodward, Clare; Barany, George (International Journal of Peptide Research and Therapeutics, 2006)

Fluorine teams up with water to restore inhibitor activity to mutant BPTI - Ye, Shijie; Loll, Bernhard; Berger, Allison Ann; Mülow, Ulrike; Alings, Claudia; Wahl, Markus Christian; Koksch, Beate (Chemical Science, 2015)
Fluorinated derivatives of aminobutyric acid engage in unique interactions with structural waters within the BPTI/trypsin interface and restore inhibitor activity. , Introducing fluorine into molecules has a wide range of effects on their physicochemical properties, often desirable but in most cases unpredictable. The fluorine atom imparts the C–F bond with low polarizability and high polarity, and significantly affects the behavior of neighboring functional groups, in a covalent or noncovalent manner. Here, we report that fluorine, present in the form of a single fluoroalkyl amino acid side chain in the P1 position of the well-characterized serine-protease inhibitor BPTI, can fully restore inhibitor activity to a mutant that contains the corresponding hydrocarbon side chain at the same site. High resolution crystal structures were obtained for four BPTI variants in complex with bovine β-trypsin, revealing changes in the stoichiometry and dynamics of water molecules in the S1 subsite. These results demonstrate that the introduction of fluorine into a protein environment can result in “chemical complementation” that has a significantly favorable impact on protein–protein interactions.

Total chemical synthesis and oxidative folding of ?-conotoxin PVIA containing an N-terminal propeptide - Buczek, Pawel; Buczek, Olga; Bulaj, Grzegorz (Biopolymers, 2005)

Amide-forming chemical ligation via O -acyl hydroxamic acids - Dunkelmann, Daniel L.; Hirata, Yuki; Totaro, Kyle A.; Cohen, Daniel T.; Zhang, Chi; Gates, Zachary P.; Pentelute, Bradley L. (Proceedings of the National Academy of Sciences, 2018)
The facile rearrangement of “ S -acyl isopeptides” to native peptide bonds via S , N -acyl shift is central to the success of native chemical ligation, the widely used approach for protein total synthesis. Proximity-driven amide bond formation via acyl transfer reactions in other contexts has proven generally less effective. Here, we show that under neutral aqueous conditions, “ O -acyl isopeptides” derived from hydroxy-asparagine [aspartic acid-β-hydroxamic acid; Asp(β-HA)] rearrange to form native peptide bonds via an O , N -acyl shift. This process constitutes a rare example of an O , N -acyl shift that proceeds rapidly across a medium-size ring (t 1/2 ∼ 15 min), and takes place in water with minimal interference from hydrolysis. In contrast to serine/threonine or tyrosine, which form O -acyl isopeptides only by the use of highly activated acyl donors and appropriate protecting groups in organic solvent, Asp(β-HA) is sufficiently reactive to form O -acyl isopeptides by treatment with an unprotected peptide- α thioester, at low mM concentration, in water. These findings were applied to an acyl transfer-based chemical ligation strategy, in which an unprotected N -terminal Asp(β-HA)-peptide and peptide- α thioester react under aqueous conditions to give a ligation product ultimately linked by a native peptide bond.

Synthetic Approaches to Disulfide-free Circular Bovine Pancreatic Trypsin Inhibitor (c-BPTI) Analogues - Tulla-Puche, Judit; Getun, Irina V.; Angell, Yvonne M.; Alsina, Jordi; Albericio, Fernando; Woodward, Clare; Barany, George (International Journal of Peptide Research and Therapeutics, 2006)

Total chemical synthesis and oxidative folding of ?-conotoxin PVIA containing an N-terminal propeptide - Buczek, Pawel; Buczek, Olga; Bulaj, Grzegorz (Biopolymers, 2005)

Fmoc-Based Synthesis of Peptide α-Thioesters Using an Aryl Hydrazine Support † - Camarero, Julio A.; Hackel, Benjamin J.; de Yoreo, James J.; Mitchell, Alexander R. (The Journal of Organic Chemistry, 2004)

Amide-forming chemical ligation via O -acyl hydroxamic acids - Dunkelmann, Daniel L.; Hirata, Yuki; Totaro, Kyle A.; Cohen, Daniel T.; Zhang, Chi; Gates, Zachary P.; Pentelute, Bradley L. (Proceedings of the National Academy of Sciences, 2018)
The facile rearrangement of “ S -acyl isopeptides” to native peptide bonds via S , N -acyl shift is central to the success of native chemical ligation, the widely used approach for protein total synthesis. Proximity-driven amide bond formation via acyl transfer reactions in other contexts has proven generally less effective. Here, we show that under neutral aqueous conditions, “ O -acyl isopeptides” derived from hydroxy-asparagine [aspartic acid-β-hydroxamic acid; Asp(β-HA)] rearrange to form native peptide bonds via an O , N -acyl shift. This process constitutes a rare example of an O , N -acyl shift that proceeds rapidly across a medium-size ring (t 1/2 ∼ 15 min), and takes place in water with minimal interference from hydrolysis. In contrast to serine/threonine or tyrosine, which form O -acyl isopeptides only by the use of highly activated acyl donors and appropriate protecting groups in organic solvent, Asp(β-HA) is sufficiently reactive to form O -acyl isopeptides by treatment with an unprotected peptide- α thioester, at low mM concentration, in water. These findings were applied to an acyl transfer-based chemical ligation strategy, in which an unprotected N -terminal Asp(β-HA)-peptide and peptide- α thioester react under aqueous conditions to give a ligation product ultimately linked by a native peptide bond.

One-pot hydrazide-based native chemical ligation for efficient chemical synthesis and structure determination of toxin Mambalgin-1 - Pan, Man; He, Yao; Wen, Ming; Wu, Fangming; Sun, Demeng; Li, Sijian; Zhang, Longhua; Li, Yiming; Tian, Changlin (Chem. Commun., 2014)
An efficient one-pot chemical synthesis of snake venom toxin Mambalgin-1 was achieved using an azide-switch strategy combined with hydrazide-based native chemical ligation. , An efficient one-pot chemical synthesis of snake venom toxin Mambalgin-1 was achieved using an azide-switch strategy combined with hydrazide-based native chemical ligation. Synthetic Mambalgin-1 exhibited a well-defined structure after sequential folding in vitro . NMR spectroscopy revealed a three-finger toxin family structure, and the synthetic toxin inhibited human acid-sensing ion channel 1a.

Chemical Synthesis, 3D Structure, and ASIC Binding Site of the Toxin Mambalgin-2 - Schroeder, Christina I.; Rash, Lachlan D.; Vila-Farrés, Xavier; Rosengren, K. Johan; Mobli, Mehdi; King, Glenn F.; Alewood, Paul F.; Craik, David J.; Durek, Thomas (Angewandte Chemie International Edition, 2014)

Fmoc-Based Synthesis of Peptide α-Thioesters Using an Aryl Hydrazine Support † - Camarero, Julio A.; Hackel, Benjamin J.; de Yoreo, James J.; Mitchell, Alexander R. (The Journal of Organic Chemistry, 2004)

One-pot hydrazide-based native chemical ligation for efficient chemical synthesis and structure determination of toxin Mambalgin-1 - Pan, Man; He, Yao; Wen, Ming; Wu, Fangming; Sun, Demeng; Li, Sijian; Zhang, Longhua; Li, Yiming; Tian, Changlin (Chem. Commun., 2014)
An efficient one-pot chemical synthesis of snake venom toxin Mambalgin-1 was achieved using an azide-switch strategy combined with hydrazide-based native chemical ligation. , An efficient one-pot chemical synthesis of snake venom toxin Mambalgin-1 was achieved using an azide-switch strategy combined with hydrazide-based native chemical ligation. Synthetic Mambalgin-1 exhibited a well-defined structure after sequential folding in vitro . NMR spectroscopy revealed a three-finger toxin family structure, and the synthetic toxin inhibited human acid-sensing ion channel 1a.

Chemical Synthesis, 3D Structure, and ASIC Binding Site of the Toxin Mambalgin-2 - Schroeder, Christina I.; Rash, Lachlan D.; Vila-Farrés, Xavier; Rosengren, K. Johan; Mobli, Mehdi; King, Glenn F.; Alewood, Paul F.; Craik, David J.; Durek, Thomas (Angewandte Chemie International Edition, 2014)

Total synthesis of mambalgin-1/2/3 by two-segment hydrazide-based native chemical ligation: Synthesis of Mambalgin by Hydrazide-based Native Chemical Ligation - Lan, Huan; Wu, Kun; Zheng, Yong; Pan, Man; Huang, Yi-Chao; Gao, Shuai; Zheng, Qing-Yun; Zheng, Ji-Shen; Li, Yi-Ming; Xiao, Bailong; Liu, Lei (Journal of Peptide Science, 2016)

Total synthesis of mambalgin-1/2/3 by two-segment hydrazide-based native chemical ligation: Synthesis of Mambalgin by Hydrazide-based Native Chemical Ligation - Lan, Huan; Wu, Kun; Zheng, Yong; Pan, Man; Huang, Yi-Chao; Gao, Shuai; Zheng, Qing-Yun; Zheng, Ji-Shen; Li, Yi-Ming; Xiao, Bailong; Liu, Lei (Journal of Peptide Science, 2016)

Cryo-EM structure of the ASIC1a–mambalgin-1 complex reveals that the peptide toxin mambalgin-1 inhibits acid-sensing ion channels through an unusual allosteric effect - Sun, Demeng; Yu, You; Xue, Xiaobin; Pan, Man; Wen, Ming; Li, Siyu; Qu, Qian; Li, Xiaorun; Zhang, Longhua; Li, Xueming; Liu, Lei; Yang, Maojun; et al. (Cell Discovery, 2018)

Cryo-EM structure of the ASIC1a–mambalgin-1 complex reveals that the peptide toxin mambalgin-1 inhibits acid-sensing ion channels through an unusual allosteric effect - Sun, Demeng; Yu, You; Xue, Xiaobin; Pan, Man; Wen, Ming; Li, Siyu; Qu, Qian; Li, Xiaorun; Zhang, Longhua; Li, Xueming; Liu, Lei; Yang, Maojun; et al. (Cell Discovery, 2018)

Homogeneous Human Complex-Type Oligosaccharides in Correctly Folded Intact Glycoproteins: Evaluation of Oligosaccharide Influence On Protein Folding, Stability, and Conformational Properties - Kajihara, Yasuhiro; Tanabe, Yasutaka; Sasaoka, Shun; Okamoto, Ryo (Chemistry - A European Journal, 2012)

Homogeneous Human Complex-Type Oligosaccharides in Correctly Folded Intact Glycoproteins: Evaluation of Oligosaccharide Influence On Protein Folding, Stability, and Conformational Properties - Kajihara, Yasuhiro; Tanabe, Yasutaka; Sasaoka, Shun; Okamoto, Ryo (Chemistry - A European Journal, 2012)

Synthesis of PAF, an Antifungal Protein from P. chrysogenum , by Native Chemical Ligation: Native Disulfide Pattern and Fold Obtained upon Oxidative Refolding - Váradi, Györgyi; Tóth, Gábor K.; Kele, Zoltán; Galgóczy, László; Fizil, Ádám; Batta, Gyula (Chemistry - A European Journal, 2013)

Synthesis of PAF, an Antifungal Protein from P. chrysogenum , by Native Chemical Ligation: Native Disulfide Pattern and Fold Obtained upon Oxidative Refolding - Váradi, Györgyi; Tóth, Gábor K.; Kele, Zoltán; Galgóczy, László; Fizil, Ádám; Batta, Gyula (Chemistry - A European Journal, 2013)

Discovery of Synthetic Penaeidin Activity against Antibiotic-resistant Fungi - Cuthbertson, Brandon J.; Büllesbach, Erika E.; Gross, Paul S. (Chemical Biology <html_ent glyph="@amp;" ascii="&"/> Drug Design, 2006)

Discovery of Synthetic Penaeidin Activity against Antibiotic-resistant Fungi - Cuthbertson, Brandon J.; Büllesbach, Erika E.; Gross, Paul S. (Chemical Biology <html_ent glyph="@amp;" ascii="&"/> Drug Design, 2006)

Chemical synthesis of dual labeled proteins via differently protected alkynes enables intramolecular FRET analysis - Hayashi, Gosuke; Kamo, Naoki; Okamoto, Akimitsu (Chemical Communications, 2017)
Differently silyl-protected alkynes enable production of a dual labeled protein through chemical protein synthesis and analysis of the protein structure by intramolecular FRET. , We report a novel method for multisite protein conjugation by setting differently silyl-protected alkynes as conjugation handles, which can remain intact through the whole synthetic procedure and provide sequential and orthogonal conjugation. This strategy enables efficient preparation of a dual dye-labeled protein and structural analysis via an intramolecular FRET mechanism.

Chemical synthesis of dual labeled proteins via differently protected alkynes enables intramolecular FRET analysis - Hayashi, Gosuke; Kamo, Naoki; Okamoto, Akimitsu (Chemical Communications, 2017)
Differently silyl-protected alkynes enable production of a dual labeled protein through chemical protein synthesis and analysis of the protein structure by intramolecular FRET. , We report a novel method for multisite protein conjugation by setting differently silyl-protected alkynes as conjugation handles, which can remain intact through the whole synthetic procedure and provide sequential and orthogonal conjugation. This strategy enables efficient preparation of a dual dye-labeled protein and structural analysis via an intramolecular FRET mechanism.

Chemical synthesis of the third WW domain of TCERG 1 by native chemical ligation - Fidan, Zerrin; Younis, Aylin; Schmieder, Peter; Volkmer, Rudolf (Journal of Peptide Science, 2011)

Chemical synthesis of the third WW domain of TCERG 1 by native chemical ligation - Fidan, Zerrin; Younis, Aylin; Schmieder, Peter; Volkmer, Rudolf (Journal of Peptide Science, 2011)

Development of a Chemical Methodology for the Preparation of Peptide Thioesters Applicable to Naturally Occurring Peptides Using a Sequential Quadruple Acyl Transfer System - Tsuda, Yusuke; Shigenaga, Akira; Tsuji, Kohei; Denda, Masaya; Sato, Kohei; Kitakaze, Keisuke; Nakamura, Takahiro; Inokuma, Tsubasa; Itoh, Kohji; Otaka, Akira (ChemistryOpen, 2015)

Development of a Chemical Methodology for the Preparation of Peptide Thioesters Applicable to Naturally Occurring Peptides Using a Sequential Quadruple Acyl Transfer System - Tsuda, Yusuke; Shigenaga, Akira; Tsuji, Kohei; Denda, Masaya; Sato, Kohei; Kitakaze, Keisuke; Nakamura, Takahiro; Inokuma, Tsubasa; Itoh, Kohji; Otaka, Akira (ChemistryOpen, 2015)

Efficient and systematic synthesis of a small glycoconjugate library having human complex type oligosaccharides - Murase, Takefumi; Tsuji, Takashi; Kajihara, Yasuhiro (Carbohydrate Research, 2009)

Efficient and systematic synthesis of a small glycoconjugate library having human complex type oligosaccharides - Murase, Takefumi; Tsuji, Takashi; Kajihara, Yasuhiro (Carbohydrate Research, 2009)

Protein Chemical Synthesis Combined with Mirror‐Image Phage Display Yields d ‐Peptide EGF Ligands that Block the EGF–EGFR Interaction - Díaz‐Perlas, Cristina; Varese, Monica; Guardiola, Salvador; Sánchez‐Navarro, Macarena; García, Jesús; Teixidó, Meritxell; Giralt, Ernest (ChemBioChem, 2019)

Protein Chemical Synthesis Combined with Mirror‐Image Phage Display Yields d ‐Peptide EGF Ligands that Block the EGF–EGFR Interaction - Díaz‐Perlas, Cristina; Varese, Monica; Guardiola, Salvador; Sánchez‐Navarro, Macarena; García, Jesús; Teixidó, Meritxell; Giralt, Ernest (ChemBioChem, 2019)

Native chemical ligation between asparagine and valine: Application and limitations for the synthesis of tri-phosphorylated C-terminal tau - Reimann, Oliver; Glanz, Maria; Hackenberger, Christian P.R. (Bioorganic & Medicinal Chemistry, 2015)

Native chemical ligation between asparagine and valine: Application and limitations for the synthesis of tri-phosphorylated C-terminal tau - Reimann, Oliver; Glanz, Maria; Hackenberger, Christian P.R. (Bioorganic & Medicinal Chemistry, 2015)

Traceless Purification and Desulfurization of Tau Protein Ligation Products - Reimann, Oliver; Smet-Nocca, Caroline; Hackenberger, Christian P. R. (Angewandte Chemie International Edition, 2015)

Traceless Purification and Desulfurization of Tau Protein Ligation Products - Reimann, Oliver; Smet-Nocca, Caroline; Hackenberger, Christian P. R. (Angewandte Chemie International Edition, 2015)

Anti-Candidal Activity and Functional Mapping of Recombinant and Synthetic Neosartorya fischeri Antifungal Protein 2 (NFAP2) - Tóth, Liliána; Váradi, Györgyi; Borics, Attila; Batta, Gyula; Kele, Zoltán; Vendrinszky, Ákos; Tóth, Roberta; Ficze, Hargita; Tóth, Gábor K.; Vágvölgyi, Csaba; Marx, Florentine; Galgóczy, László (Frontiers in Microbiology, 2018)

Anti-Candidal Activity and Functional Mapping of Recombinant and Synthetic Neosartorya fischeri Antifungal Protein 2 (NFAP2) - Tóth, Liliána; Váradi, Györgyi; Borics, Attila; Batta, Gyula; Kele, Zoltán; Vendrinszky, Ákos; Tóth, Roberta; Ficze, Hargita; Tóth, Gábor K.; Vágvölgyi, Csaba; Marx, Florentine; Galgóczy, László (Frontiers in Microbiology, 2018)

His6 tag-assisted chemical protein synthesis - Bang, D.; Kent, S. B. H. (Proceedings of the National Academy of Sciences, 2005)

His6 tag-assisted chemical protein synthesis - Bang, D.; Kent, S. B. H. (Proceedings of the National Academy of Sciences, 2005)

Design and Folding of [GluA4(OβThrB30)]Insulin (“Ester Insulin”): A Minimal Proinsulin Surrogate that Can Be Chemically Converted into Human Insulin - Sohma, Youhei; Hua, Qing-Xin; Whittaker, Jonathan; Weiss, Michael A.; Kent, Stephen B. H. (Angewandte Chemie International Edition, 2010)

Design and Folding of [GluA4(OβThrB30)]Insulin (“Ester Insulin”): A Minimal Proinsulin Surrogate that Can Be Chemically Converted into Human Insulin - Sohma, Youhei; Hua, Qing-Xin; Whittaker, Jonathan; Weiss, Michael A.; Kent, Stephen B. H. (Angewandte Chemie International Edition, 2010)

Design and Folding of [GluA4(OβThrB30)]Insulin (“Ester Insulin”): A Minimal Proinsulin Surrogate that Can Be Chemically Converted into Human Insulin - Sohma, Youhei; Hua, Qing-Xin; Whittaker, Jonathan; Weiss, Michael A.; Kent, Stephen B. H. (Angewandte Chemie, 2010)

Comparative Total Syntheses of Turkey Ovomucoid Third Domain by Both Stepwise Solid Phase Peptide Synthesis and Native Chemical Ligation - Lu, Wuyuan; Qasim, M. A.; Kent, Stephen B. H. (Journal of the American Chemical Society, 1996)

Design and Folding of [GluA4(OβThrB30)]Insulin (“Ester Insulin”): A Minimal Proinsulin Surrogate that Can Be Chemically Converted into Human Insulin - Sohma, Youhei; Hua, Qing-Xin; Whittaker, Jonathan; Weiss, Michael A.; Kent, Stephen B. H. (Angewandte Chemie, 2010)

Synthesis of protein kinase Cδ C1b domain by native chemical ligation methodology and characterization of its folding and ligand binding - Ohashi, Nami; Nomura, Wataru; Kato, Mai; Narumi, Tetsuo; Lewin, Nancy E.; Blumberg, Peter M.; Tamamura, Hirokazu (Journal of Peptide Science, 2009)

Comparative Total Syntheses of Turkey Ovomucoid Third Domain by Both Stepwise Solid Phase Peptide Synthesis and Native Chemical Ligation - Lu, Wuyuan; Qasim, M. A.; Kent, Stephen B. H. (Journal of the American Chemical Society, 1996)

Synthesis of protein kinase Cδ C1b domain by native chemical ligation methodology and characterization of its folding and ligand binding - Ohashi, Nami; Nomura, Wataru; Kato, Mai; Narumi, Tetsuo; Lewin, Nancy E.; Blumberg, Peter M.; Tamamura, Hirokazu (Journal of Peptide Science, 2009)

Efficient Total Chemical Synthesis of 13 C= 18 O Isotopomers of Human Insulin for Isotope-Edited FTIR - Dhayalan, Balamurugan; Fitzpatrick, Ann; Mandal, Kalyaneswar; Whittaker, Jonathan; Weiss, Michael A.; Tokmakoff, Andrei; Kent, Stephen B. H. (ChemBioChem, 2016)

Efficient Total Chemical Synthesis of 13 C= 18 O Isotopomers of Human Insulin for Isotope-Edited FTIR - Dhayalan, Balamurugan; Fitzpatrick, Ann; Mandal, Kalyaneswar; Whittaker, Jonathan; Weiss, Michael A.; Tokmakoff, Andrei; Kent, Stephen B. H. (ChemBioChem, 2016)

Native Chemical Ligation Strategy to Overcome Side Reactions during Fmoc-Based Synthesis of C-Terminal Cysteine-Containing Peptides - Lelièvre, Dominique; Terrier, Victor P.; Delmas, Agnès F.; Aucagne, Vincent (Organic Letters, 2016)

Native Chemical Ligation Strategy to Overcome Side Reactions during Fmoc-Based Synthesis of C-Terminal Cysteine-Containing Peptides - Lelièvre, Dominique; Terrier, Victor P.; Delmas, Agnès F.; Aucagne, Vincent (Organic Letters, 2016)

Scope and Limitations of Fmoc Chemistry SPPS-Based Approaches to the Total Synthesis of Insulin Lispro via Ester Insulin - Dhayalan, Balamurugan; Mandal, Kalyaneswar; Rege, Nischay; Weiss, Michael A.; Eitel, Simon H.; Meier, Thomas; Schoenleber, Ralph O.; Kent, Stephen B. H. (Chemistry - A European Journal, 2017)

Scope and Limitations of Fmoc Chemistry SPPS-Based Approaches to the Total Synthesis of Insulin Lispro via Ester Insulin - Dhayalan, Balamurugan; Mandal, Kalyaneswar; Rege, Nischay; Weiss, Michael A.; Eitel, Simon H.; Meier, Thomas; Schoenleber, Ralph O.; Kent, Stephen B. H. (Chemistry - A European Journal, 2017)

Chemical synthesis of membrane proteins: a model study on the influenza virus B proton channel - Baumruck, A. C.; Tietze, D.; Steinacker, L. K.; Tietze, A. A. (Chemical Science, 2018)
NCL results in the quantitative yield of a membrane protein, where a thioester peptide is formed from an oxo-ester with an in situ cleavable solubilizing tag. , In the present study we have developed and optimized a robust strategy for the synthesis of highly hydrophobic peptides, especially membrane proteins, exemplarily using the influenza B M2 proton channel (BM2(1–51)). This strategy is based on the native chemical ligation of two fragments, where the thioester fragment is formed from an oxo-ester peptide, which is synthesized using Fmoc-SPPS, and features an in situ cleavable solubilizing tag (ADO, ADO 2 or ADO-Lys 5 ). The nearly quantitative production of the ligation product was followed by an optimized work up protocol, resulting in almost quantitative desulfurization and Acm-group cleavage. Circular dichroism analysis in a POPC lipid membrane revealed that the synthetic BM2(1–51) construct adopts a helical structure similar to that of the previously characterized BM2(1–33).

Chemical synthesis of membrane proteins: a model study on the influenza virus B proton channel - Baumruck, A. C.; Tietze, D.; Steinacker, L. K.; Tietze, A. A. (Chemical Science, 2018)
NCL results in the quantitative yield of a membrane protein, where a thioester peptide is formed from an oxo-ester with an in situ cleavable solubilizing tag. , In the present study we have developed and optimized a robust strategy for the synthesis of highly hydrophobic peptides, especially membrane proteins, exemplarily using the influenza B M2 proton channel (BM2(1–51)). This strategy is based on the native chemical ligation of two fragments, where the thioester fragment is formed from an oxo-ester peptide, which is synthesized using Fmoc-SPPS, and features an in situ cleavable solubilizing tag (ADO, ADO 2 or ADO-Lys 5 ). The nearly quantitative production of the ligation product was followed by an optimized work up protocol, resulting in almost quantitative desulfurization and Acm-group cleavage. Circular dichroism analysis in a POPC lipid membrane revealed that the synthetic BM2(1–51) construct adopts a helical structure similar to that of the previously characterized BM2(1–33).

Facile folding of insulin variants bearing a prosthetic C-peptide prepared by α-ketoacid-hydroxylamine (KAHA) ligation - Boross, Gábor N.; Shimura, Satomi; Besenius, Melissa; Tennagels, Norbert; Rossen, Kai; Wagner, Michael; Bode, Jeffrey W. (Chemical Science, 2018)
Ester forming KAHA-ligation and a traceless prosthetic C-peptide provides a modular platform for the synthesis and folding of insulin variants. , The chemical synthesis of insulin is an enduring challenge due to the hydrophobic peptide chains and construction of the correct intermolecular disulfide pattern. We report a new approach to the chemical synthesis of insulin using a short, traceless, prosthetic C-peptide that facilitates the formation of the correct disulfide pattern during folding and its removal by basic treatment. The linear precursor is assembled by an ester forming α-ketoacid-hydroxylamine (KAHA) ligation that provides access to the linear insulin precursors in good yield from two readily prepared segments. This convergent and flexible route provides access to various human, mouse, and guinea pig insulins containing a single homoserine mutation that shows no detrimental effect on the biological activities.

Facile folding of insulin variants bearing a prosthetic C-peptide prepared by α-ketoacid-hydroxylamine (KAHA) ligation - Boross, Gábor N.; Shimura, Satomi; Besenius, Melissa; Tennagels, Norbert; Rossen, Kai; Wagner, Michael; Bode, Jeffrey W. (Chemical Science, 2018)
Ester forming KAHA-ligation and a traceless prosthetic C-peptide provides a modular platform for the synthesis and folding of insulin variants. , The chemical synthesis of insulin is an enduring challenge due to the hydrophobic peptide chains and construction of the correct intermolecular disulfide pattern. We report a new approach to the chemical synthesis of insulin using a short, traceless, prosthetic C-peptide that facilitates the formation of the correct disulfide pattern during folding and its removal by basic treatment. The linear precursor is assembled by an ester forming α-ketoacid-hydroxylamine (KAHA) ligation that provides access to the linear insulin precursors in good yield from two readily prepared segments. This convergent and flexible route provides access to various human, mouse, and guinea pig insulins containing a single homoserine mutation that shows no detrimental effect on the biological activities.

The versatile use of solubilizing trityl tags for difficult peptide/protein synthesis - Tsuda, Shugo; Masuda, Shun; Yoshiya, Taku (Organic & Biomolecular Chemistry, 2019)
Our solubilizing trityl tags designed for difficult peptide/protein synthesis proved applicable to metal-free radical-triggered desulfurization and an Ag-mediated thioester method. , Solubilizing trityl tags (Trt-oligoLys/Arg) proved applicable to metal-free radical-triggered desulfurization and an Ag-mediated thioester method. Additionally, using the solubilizing trityl tag strategy, synthesis of the influenza BM2 proton channel, which previously required organic solvent-aided native chemical ligation (NCL) and desulfurization due to its low solubility, was achieved without using organic solvents.

The versatile use of solubilizing trityl tags for difficult peptide/protein synthesis - Tsuda, Shugo; Masuda, Shun; Yoshiya, Taku (Organic & Biomolecular Chemistry, 2019)
Our solubilizing trityl tags designed for difficult peptide/protein synthesis proved applicable to metal-free radical-triggered desulfurization and an Ag-mediated thioester method. , Solubilizing trityl tags (Trt-oligoLys/Arg) proved applicable to metal-free radical-triggered desulfurization and an Ag-mediated thioester method. Additionally, using the solubilizing trityl tag strategy, synthesis of the influenza BM2 proton channel, which previously required organic solvent-aided native chemical ligation (NCL) and desulfurization due to its low solubility, was achieved without using organic solvents.

Chemical ligation of the influenza M2 protein for solid-state NMR characterization of the cytoplasmic domain: Chemical Ligation of Influenza M2 for SSNMR - Kwon, Byungsu; Tietze, Daniel; White, Paul B.; Liao, Shu Y.; Hong, Mei (Protein Science, 2015)

Chemical ligation of the influenza M2 protein for solid-state NMR characterization of the cytoplasmic domain: Chemical Ligation of Influenza M2 for SSNMR - Kwon, Byungsu; Tietze, Daniel; White, Paul B.; Liao, Shu Y.; Hong, Mei (Protein Science, 2015)

Determination of the X-ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallography: X-ray Crystal Structure Determination of Racemic Omwaprin - Banigan, James R.; Mandal, Kalyaneswar; Sawaya, Michael R.; Thammavongsa, Vilasak; Hendrickx, Antoni P. A.; Schneewind, Olaf; Yeates, Todd O.; Kent, Stephen B. H. (Protein Science, 2010)

Determination of the X-ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallography: X-ray Crystal Structure Determination of Racemic Omwaprin - Banigan, James R.; Mandal, Kalyaneswar; Sawaya, Michael R.; Thammavongsa, Vilasak; Hendrickx, Antoni P. A.; Schneewind, Olaf; Yeates, Todd O.; Kent, Stephen B. H. (Protein Science, 2010)

Holocyclotoxin-1, a cystine knot toxin from Ixodes holocyclus - Vink, Simone; Daly, Norelle L.; Steen, Natalie; Craik, David J.; Alewood, Paul F. (Toxicon, 2014)

Holocyclotoxin-1, a cystine knot toxin from Ixodes holocyclus - Vink, Simone; Daly, Norelle L.; Steen, Natalie; Craik, David J.; Alewood, Paul F. (Toxicon, 2014)

Chemoselective derivitization of folded synthetic insulin variants with potassium acyltrifluoroborates (KATs) - Boross, Gabor N.; Schauenburg, Dominik; Bode, Jeffrey W. (Helvetica Chimica Acta, 2018)

Chemoselective derivitization of folded synthetic insulin variants with potassium acyltrifluoroborates (KATs) - Boross, Gabor N.; Schauenburg, Dominik; Bode, Jeffrey W. (Helvetica Chimica Acta, 2018)

Efficient synthesis of longer Aβ peptides via removable backbone modification - Zuo, Chao; Tang, Shan; Si, Yan-Yan; Wang, Zhipeng A.; Tian, Chang-Lin; Zheng, Ji-Shen (Organic & Biomolecular Chemistry, 2016)
This paper describes a new method for the efficient chemical synthesis of longer Aβ peptides with the combination of the RBM strategy and native chemical ligation. , Longer amyloid-beta (Aβ) peptides (43 to 49 amino acids) play essential roles in the pathology of Alzheimer's disease (AD). The difficulty in the preparation of longer Aβ peptides is still an obstacle to elucidate their roles in AD. Herein we report a robust and efficient strategy for the chemical synthesis of longer Aβ peptides (Aβ48 and Aβ49). A key feature of this method is the installation of removable Arg 4 -tagged backbone modification groups into the hydrophobic region of Aβ. This modification can improve the handling properties of the purification, ligation and mass characterization of longer Aβ peptides. The practicability of the new method has been demonstrated by the successful synthesis of Aβ48 and Aβ49 peptides.

Efficient synthesis of longer Aβ peptides via removable backbone modification - Zuo, Chao; Tang, Shan; Si, Yan-Yan; Wang, Zhipeng A.; Tian, Chang-Lin; Zheng, Ji-Shen (Organic & Biomolecular Chemistry, 2016)
This paper describes a new method for the efficient chemical synthesis of longer Aβ peptides with the combination of the RBM strategy and native chemical ligation. , Longer amyloid-beta (Aβ) peptides (43 to 49 amino acids) play essential roles in the pathology of Alzheimer's disease (AD). The difficulty in the preparation of longer Aβ peptides is still an obstacle to elucidate their roles in AD. Herein we report a robust and efficient strategy for the chemical synthesis of longer Aβ peptides (Aβ48 and Aβ49). A key feature of this method is the installation of removable Arg 4 -tagged backbone modification groups into the hydrophobic region of Aβ. This modification can improve the handling properties of the purification, ligation and mass characterization of longer Aβ peptides. The practicability of the new method has been demonstrated by the successful synthesis of Aβ48 and Aβ49 peptides.

A Type of Auxiliary for Native Chemical Peptide Ligation beyond Cysteine and Glycine Junctions - Loibl, Simon F.; Harpaz, Ziv; Seitz, Oliver (Angewandte Chemie International Edition, 2015)

A Type of Auxiliary for Native Chemical Peptide Ligation beyond Cysteine and Glycine Junctions - Loibl, Simon F.; Harpaz, Ziv; Seitz, Oliver (Angewandte Chemie International Edition, 2015)

Native chemical ligation at a base-labile 4-mercaptobutyrate Nα-auxiliary - Harpaz, Ziv; Loibl, Simon; Seitz, Oliver (Bioorganic & Medicinal Chemistry Letters, 2016)

Native chemical ligation at a base-labile 4-mercaptobutyrate Nα-auxiliary - Harpaz, Ziv; Loibl, Simon; Seitz, Oliver (Bioorganic & Medicinal Chemistry Letters, 2016)

Design, Total Chemical Synthesis, and X-Ray Structure of a Protein Having a Novel Linear-Loop Polypeptide Chain Topology - Mandal, Kalyaneswar; Pentelute, Brad L.; Bang, Duhee; Gates, Zachary P.; Torbeev, Vladimir Yu.; Kent, Stephen B. H. (Angewandte Chemie International Edition, 2012)

Design, Total Chemical Synthesis, and X-Ray Structure of a Protein Having a Novel Linear-Loop Polypeptide Chain Topology - Mandal, Kalyaneswar; Pentelute, Brad L.; Bang, Duhee; Gates, Zachary P.; Torbeev, Vladimir Yu.; Kent, Stephen B. H. (Angewandte Chemie International Edition, 2012)

Chemical Protein Synthesis by Kinetically Controlled Ligation of Peptide O-Esters - Zheng, Ji-Shen; Cui, Hong-Kui; Fang, Ge-Min; Xi, Wei-Xian; Liu, Lei (ChemBioChem, 2010)

Chemical Protein Synthesis by Kinetically Controlled Ligation of Peptide O-Esters - Zheng, Ji-Shen; Cui, Hong-Kui; Fang, Ge-Min; Xi, Wei-Xian; Liu, Lei (ChemBioChem, 2010)

Evaluation of the effect of post‐translational modification toward protein structure: Chemical synthesis of glycosyl crambins having either a high mannose‐type or a complex‐type oligosaccharide - Dedola, Simone; Izumi, Masayuki; Makimura, Yutaka; Ito, Yukishige; Kajihara, Yasuhiro (Peptide Science, 2016)

Evaluation of the effect of post‐translational modification toward protein structure: Chemical synthesis of glycosyl crambins having either a high mannose‐type or a complex‐type oligosaccharide - Dedola, Simone; Izumi, Masayuki; Makimura, Yutaka; Ito, Yukishige; Kajihara, Yasuhiro (Peptide Science, 2016)

Kinetically Controlled Ligation for the Convergent Chemical Synthesis of Proteins - Bang, Duhee; Pentelute, Brad L.; Kent, Stephen B. H. (Angewandte Chemie International Edition, 2006)

Kinetically Controlled Ligation for the Convergent Chemical Synthesis of Proteins - Bang, Duhee; Pentelute, Brad L.; Kent, Stephen B. H. (Angewandte Chemie International Edition, 2006)

Total Chemical Synthesis of Crambin - Bang, Duhee; Chopra, Neeraj; Kent, Stephen B. H. (Journal of the American Chemical Society, 2004)

Total Chemical Synthesis of Crambin - Bang, Duhee; Chopra, Neeraj; Kent, Stephen B. H. (Journal of the American Chemical Society, 2004)

A One-Pot Total Synthesis of Crambin - Bang, Duhee; Kent, Stephen B. H. (Angewandte Chemie International Edition, 2004)

A One-Pot Total Synthesis of Crambin - Bang, Duhee; Kent, Stephen B. H. (Angewandte Chemie International Edition, 2004)

A Highly Efficient Method for Site-Specific Modification of Unprotected Peptides after Chemical Synthesis - Bark, Steven J.; Schmid, Sandra; Hahn, Klaus M. (Journal of the American Chemical Society, 2000)

A Highly Efficient Method for Site-Specific Modification of Unprotected Peptides after Chemical Synthesis - Bark, Steven J.; Schmid, Sandra; Hahn, Klaus M. (Journal of the American Chemical Society, 2000)

Peptide thioester synthesis through N→S acyl-transfer: application to the synthesis of a β-defensin - Kang, Jaskiranjit; Reynolds, Natalie L.; Tyrrell, Christine; Dorin, Julia R.; Macmillan, Derek (Organic & Biomolecular Chemistry, 2009)

Peptide thioester synthesis through N→S acyl-transfer: application to the synthesis of a β-defensin - Kang, Jaskiranjit; Reynolds, Natalie L.; Tyrrell, Christine; Dorin, Julia R.; Macmillan, Derek (Organic & Biomolecular Chemistry, 2009)

Evaluation of Chemical Strategies for Improving the Stability and Oral Toxicity of Insecticidal Peptides - Herzig, Volker; de Araujo, Aline; Greenwood, Kathryn; Chin, Yanni; Windley, Monique; Chong, Youmie; Muttenthaler, Markus; Mobli, Mehdi; Audsley, Neil; Nicholson, Graham; Alewood, Paul; King, Glenn (Biomedicines, 2018)
Spider venoms are a rich source of insecticidal peptide toxins. Their development as bioinsecticides has, however, been hampered due to concerns about potential lack of stability and oral bioactivity. We therefore systematically evaluated several synthetic strategies to increase the stability and oral potency of the potent insecticidal spider-venom peptide ω-HXTX-Hv1a (Hv1a). Selective chemical replacement of disulfide bridges with diselenide bonds and N- to C-terminal cyclization were anticipated to improve Hv1a resistance to proteolytic digestion, and thereby its activity when delivered orally. We found that native Hv1a is orally active in blowflies, but 91-fold less potent than when administered by injection. Introduction of a single diselenide bond had no effect on the susceptibility to scrambling or the oral activity of Hv1a. N- to C-terminal cyclization of the peptide backbone did not significantly improve the potency of Hv1a when injected into blowflies and it led to a significant decrease in oral activity. We show that this is likely due to a dramatically reduced rate of translocation of cyclic Hv1a across the insect midgut, highlighting the importance of testing bioavailability in addition to toxin stability.

Evaluation of Chemical Strategies for Improving the Stability and Oral Toxicity of Insecticidal Peptides - Herzig, Volker; de Araujo, Aline; Greenwood, Kathryn; Chin, Yanni; Windley, Monique; Chong, Youmie; Muttenthaler, Markus; Mobli, Mehdi; Audsley, Neil; Nicholson, Graham; Alewood, Paul; King, Glenn (Biomedicines, 2018)
Spider venoms are a rich source of insecticidal peptide toxins. Their development as bioinsecticides has, however, been hampered due to concerns about potential lack of stability and oral bioactivity. We therefore systematically evaluated several synthetic strategies to increase the stability and oral potency of the potent insecticidal spider-venom peptide ω-HXTX-Hv1a (Hv1a). Selective chemical replacement of disulfide bridges with diselenide bonds and N- to C-terminal cyclization were anticipated to improve Hv1a resistance to proteolytic digestion, and thereby its activity when delivered orally. We found that native Hv1a is orally active in blowflies, but 91-fold less potent than when administered by injection. Introduction of a single diselenide bond had no effect on the susceptibility to scrambling or the oral activity of Hv1a. N- to C-terminal cyclization of the peptide backbone did not significantly improve the potency of Hv1a when injected into blowflies and it led to a significant decrease in oral activity. We show that this is likely due to a dramatically reduced rate of translocation of cyclic Hv1a across the insect midgut, highlighting the importance of testing bioavailability in addition to toxin stability.

Synthesis of human growth hormone-releasing hormone via three-fragment serine/threonine ligation (STL) - Zhang, Yinfeng; Li, Tianlu; Li, Xuechen (Organic & Biomolecular Chemistry, 2013)

Synthesis of human growth hormone-releasing hormone via three-fragment serine/threonine ligation (STL) - Zhang, Yinfeng; Li, Tianlu; Li, Xuechen (Organic & Biomolecular Chemistry, 2013)

Native Chemical Ligation–Photodesulfurization in Flow - Chisholm, Timothy S.; Clayton, Daniel; Dowman, Luke J.; Sayers, Jessica; Payne, Richard J. (Journal of the American Chemical Society, 2018)

Native Chemical Ligation–Photodesulfurization in Flow - Chisholm, Timothy S.; Clayton, Daniel; Dowman, Luke J.; Sayers, Jessica; Payne, Richard J. (Journal of the American Chemical Society, 2018)

Synthesis of the Antimicrobial S-Linked Glycopeptide, Glycocin F - Brimble, Margaret A.; Edwards, Pat J.; Harris, Paul W. R.; Norris, Gillian E.; Patchett, Mark L.; Wright, Tom H.; Yang, Sung-Hyun; Carley, Sarah E. (Chemistry - A European Journal, 2015)

Rapid Parallel Synthesis of Bioactive Folded Cyclotides by Using a Tea-Bag Approach - Aboye, Teshome; Kuang, Yuting; Neamati, Nouri; Camarero, Julio A. (ChemBioChem, 2015)

Synthesis of the Antimicrobial S-Linked Glycopeptide, Glycocin F - Brimble, Margaret A.; Edwards, Pat J.; Harris, Paul W. R.; Norris, Gillian E.; Patchett, Mark L.; Wright, Tom H.; Yang, Sung-Hyun; Carley, Sarah E. (Chemistry - A European Journal, 2015)

Rapid Parallel Synthesis of Bioactive Folded Cyclotides by Using a Tea-Bag Approach - Aboye, Teshome; Kuang, Yuting; Neamati, Nouri; Camarero, Julio A. (ChemBioChem, 2015)

Total chemical synthesis of glycocin F and analogues: S -glycosylation confers improved antimicrobial activity - Amso, Zaid; Bisset, Sean W.; Yang, Sung-Hyun; Harris, Paul W. R.; Wright, Tom H.; Navo, Claudio D.; Patchett, Mark L.; Norris, Gillian E.; Brimble, Margaret A. (Chemical Science, 2018)
Replacing the O -linked saccharide in the bacteriocin glycocin F with an S -linked version results in a peptidomimetic that increases the bacteriostatic effect. , Glycocin F (GccF) is a unique diglycosylated bacteriocin peptide that possesses potent and reversible bacteriostatic activity against a range of Gram-positive bacteria. GccF is a rare example of a ‘glycoactive’ bacteriocin, with both the O -linked N -acetylglucosamine (GlcNAc) and the unusual S -linked GlcNAc moiety important for antibacterial activity. In this report, glycocin F was successfully prepared using a native chemical ligation strategy and folded into its native structure. The chemically synthesised glycocin appeared to be slightly more active than the recombinant material produced from Lactobacillus plantarum . A second-generation synthetic strategy was used to prepare 2 site selective ‘glyco-mutants’ containing either two S -linked or two O -linked GlcNAc moieties; these mutants were used to probe the contribution of each type of glycosidic linkage to bacteriostatic activity. Replacing the S -linked GlcNAc at residue 43 with an O -linked GlcNAc decreased the antibacterial activity, while replacing O -linked GlcNAc at position 18 with an S -linked GlcNAc increased the bioactivity suggesting that the S -glycosidic linkage may offer a biologically-inspired route towards more active bacteriocins.

Total chemical synthesis of glycocin F and analogues: S -glycosylation confers improved antimicrobial activity - Amso, Zaid; Bisset, Sean W.; Yang, Sung-Hyun; Harris, Paul W. R.; Wright, Tom H.; Navo, Claudio D.; Patchett, Mark L.; Norris, Gillian E.; Brimble, Margaret A. (Chemical Science, 2018)
Replacing the O -linked saccharide in the bacteriocin glycocin F with an S -linked version results in a peptidomimetic that increases the bacteriostatic effect. , Glycocin F (GccF) is a unique diglycosylated bacteriocin peptide that possesses potent and reversible bacteriostatic activity against a range of Gram-positive bacteria. GccF is a rare example of a ‘glycoactive’ bacteriocin, with both the O -linked N -acetylglucosamine (GlcNAc) and the unusual S -linked GlcNAc moiety important for antibacterial activity. In this report, glycocin F was successfully prepared using a native chemical ligation strategy and folded into its native structure. The chemically synthesised glycocin appeared to be slightly more active than the recombinant material produced from Lactobacillus plantarum . A second-generation synthetic strategy was used to prepare 2 site selective ‘glyco-mutants’ containing either two S -linked or two O -linked GlcNAc moieties; these mutants were used to probe the contribution of each type of glycosidic linkage to bacteriostatic activity. Replacing the S -linked GlcNAc at residue 43 with an O -linked GlcNAc decreased the antibacterial activity, while replacing O -linked GlcNAc at position 18 with an S -linked GlcNAc increased the bioactivity suggesting that the S -glycosidic linkage may offer a biologically-inspired route towards more active bacteriocins.

Native Chemical Ligation at Serine Revisited - Snella, Benoît; Diemer, Vincent; Drobecq, Hervé; Agouridas, Vangelis; Melnyk, Oleg (Organic Letters, 2018)

Native Chemical Ligation at Serine Revisited - Snella, Benoît; Diemer, Vincent; Drobecq, Hervé; Agouridas, Vangelis; Melnyk, Oleg (Organic Letters, 2018)

Using Chemical Synthesis to Probe Structure–Activity Relationships of the Glycoactive Bacteriocin Glycocin F - Bisset, Sean W.; Yang, Sung-Hyun; Amso, Zaid; Harris, Paul W. R.; Patchett, Mark L.; Brimble, Margaret A.; Norris, Gillian E. (ACS Chemical Biology, 2018)

Using Chemical Synthesis to Probe Structure–Activity Relationships of the Glycoactive Bacteriocin Glycocin F - Bisset, Sean W.; Yang, Sung-Hyun; Amso, Zaid; Harris, Paul W. R.; Patchett, Mark L.; Brimble, Margaret A.; Norris, Gillian E. (ACS Chemical Biology, 2018)

Combination of Thiol-Additive-Free Native Chemical Ligation/Desulfurization and Intentional Replacement of Alanine with Cysteine - Tsuda, Shugo; Mochizuki, Masayoshi; Nishio, Hideki; Yoshiya, Taku (ChemBioChem, 2016)

Combination of Thiol-Additive-Free Native Chemical Ligation/Desulfurization and Intentional Replacement of Alanine with Cysteine - Tsuda, Shugo; Mochizuki, Masayoshi; Nishio, Hideki; Yoshiya, Taku (ChemBioChem, 2016)

Construction of Ribonuclease-Decorated Artificial Virus-like Capsid by Peptide Self-assembly - Matsuura, Kazunori; Ota, Junpei; Fujita, Seiya; Shiomi, Yuriko; Inaba, Hiroshi (The Journal of Organic Chemistry, 2020)

Construction of Ribonuclease-Decorated Artificial Virus-like Capsid by Peptide Self-assembly - Matsuura, Kazunori; Ota, Junpei; Fujita, Seiya; Shiomi, Yuriko; Inaba, Hiroshi (The Journal of Organic Chemistry, 2020)

Hydrazine-Sensitive Thiol Protecting Group for Peptide and Protein Chemistry - Shen, Fei; Zhang, Zhi-Ping; Li, Jia-Bin; Lin, Yun; Liu, Lei (Organic Letters, 2011)

Hydrazine-Sensitive Thiol Protecting Group for Peptide and Protein Chemistry - Shen, Fei; Zhang, Zhi-Ping; Li, Jia-Bin; Lin, Yun; Liu, Lei (Organic Letters, 2011)

Facile and efficient chemical synthesis of APET×2, an ASIC-targeting toxin, via hydrazide-based native chemical ligation - Li, Si-Jian; Qu, Da-Liang; Wang, Ye-Hai; He, Yao; Wen, Min; Guo, Qing-Xiang; Shi, Jing; Li, Yi-Ming (Tetrahedron, 2015)

Facile and efficient chemical synthesis of APET×2, an ASIC-targeting toxin, via hydrazide-based native chemical ligation - Li, Si-Jian; Qu, Da-Liang; Wang, Ye-Hai; He, Yao; Wen, Min; Guo, Qing-Xiang; Shi, Jing; Li, Yi-Ming (Tetrahedron, 2015)

Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel 3 - Jensen, Jonas E.; Durek, Thomas; Alewood, Paul F.; Adams, David J.; King, Glenn F.; Rash, Lachlan D. (Toxicon, 2009)

Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel 3 - Jensen, Jonas E.; Durek, Thomas; Alewood, Paul F.; Adams, David J.; King, Glenn F.; Rash, Lachlan D. (Toxicon, 2009)

Synthesis of a secretoglobin 3A2 type C (98–139) fragment by Dawson’s native chemical ligation - Kikuchi, Mariko; Kurotani, Reiko; Konno, Hiroyuki (Tetrahedron Letters, 2017)

Synthesis of a secretoglobin 3A2 type C (98–139) fragment by Dawson’s native chemical ligation - Kikuchi, Mariko; Kurotani, Reiko; Konno, Hiroyuki (Tetrahedron Letters, 2017)

An efficient solid-phase synthesis of peptidyl- N -acetylguanidines for use in native chemical ligation: An Efficient Solid-Phase Synthesis of Peptidyl- N -Acetylguanidines - Okamoto, Ryo; Isoe, Madoka; Izumi, Masayuki; Kajihara, Yasuhiro (Journal of Peptide Science, 2016)

An efficient solid-phase synthesis of peptidyl- N -acetylguanidines for use in native chemical ligation: An Efficient Solid-Phase Synthesis of Peptidyl- N -Acetylguanidines - Okamoto, Ryo; Isoe, Madoka; Izumi, Masayuki; Kajihara, Yasuhiro (Journal of Peptide Science, 2016)

Solubilizing Trityl‐Type Tag To Synthesize Asx/Glx‐Containing Peptides - Tsuda, Shugo; Masuda, Shun; Yoshiya, Taku (ChemBioChem, 2019)

Solubilizing Trityl‐Type Tag To Synthesize Asx/Glx‐Containing Peptides - Tsuda, Shugo; Masuda, Shun; Yoshiya, Taku (ChemBioChem, 2019)

A PEGylated Photocleavable Auxiliary Mediates the Sequential Enzymatic Glycosylation and Native Chemical Ligation of Peptides - Bello, Claudia; Wang, Shuo; Meng, Lu; Moremen, Kelley W.; Becker, Christian F. W. (Angewandte Chemie International Edition, 2015)

A PEGylated Photocleavable Auxiliary Mediates the Sequential Enzymatic Glycosylation and Native Chemical Ligation of Peptides - Bello, Claudia; Wang, Shuo; Meng, Lu; Moremen, Kelley W.; Becker, Christian F. W. (Angewandte Chemie International Edition, 2015)

One-Pot/Sequential Native Chemical Ligation Using Photocaged Crypto-thioester - Aihara, Keisuke; Yamaoka, Kosuke; Naruse, Naoto; Inokuma, Tsubasa; Shigenaga, Akira; Otaka, Akira (Organic Letters, 2016)

One-Pot/Sequential Native Chemical Ligation Using Photocaged Crypto-thioester - Aihara, Keisuke; Yamaoka, Kosuke; Naruse, Naoto; Inokuma, Tsubasa; Shigenaga, Akira; Otaka, Akira (Organic Letters, 2016)

Native Chemical Ligation to Minimize Aspartimide Formation during Chemical Synthesis of Small LDLa Protein - Tailhades, Julien; Sethi, Ashish; Petrie, Emma J.; Gooley, Paul R.; Bathgate, Ross A.; Wade, John D.; Hossain, Mohammed A. (Chemistry - A European Journal, 2016)

Native Chemical Ligation to Minimize Aspartimide Formation during Chemical Synthesis of Small LDLa Protein - Tailhades, Julien; Sethi, Ashish; Petrie, Emma J.; Gooley, Paul R.; Bathgate, Ross A.; Wade, John D.; Hossain, Mohammed A. (Chemistry - A European Journal, 2016)

Toward the total chemical synthesis of the cancer protein NY-ESO-1 - Harris, Paul W. R.; Brimble, Margaret A. (Biopolymers, 2010)

Toward the total chemical synthesis of the cancer protein NY-ESO-1 - Harris, Paul W. R.; Brimble, Margaret A. (Biopolymers, 2010)

Expanding the Scope of Native Chemical Ligation in Glycopeptide Synthesis - Okamoto, Ryo; Izumi, Masayuki; Kajihara, Yasuhiro (International Journal of Peptide Research and Therapeutics, 2010)

Expanding the Scope of Native Chemical Ligation in Glycopeptide Synthesis - Okamoto, Ryo; Izumi, Masayuki; Kajihara, Yasuhiro (International Journal of Peptide Research and Therapeutics, 2010)

Novel semisynthetic method for generating full length β-amyloid peptides - Bockhorn, Jessica J.; Lazar, Kristi L.; Gasser, Adam J.; Luther, Laura M.; Qahwash, Isam M.; Chopra, Neeraj; Meredith, Stephen C. (Biopolymers, 2010)

Novel semisynthetic method for generating full length β-amyloid peptides - Bockhorn, Jessica J.; Lazar, Kristi L.; Gasser, Adam J.; Luther, Laura M.; Qahwash, Isam M.; Chopra, Neeraj; Meredith, Stephen C. (Biopolymers, 2010)

Native Chemical Ligation at Glutamine - Siman, Peter; Karthikeyan, Subramanian Vedhanarayanan; Brik, Ashraf (Organic Letters, 2012)

Solid-Phase Synthesis of Peptide and Glycopeptide Thioesters through Side-Chain-Anchoring Strategies - Ficht, Simon; Payne, Richard J.; Guy, Richard T.; Wong, Chi-Huey (Chemistry - A European Journal, 2008)

Native Chemical Ligation at Glutamine - Siman, Peter; Karthikeyan, Subramanian Vedhanarayanan; Brik, Ashraf (Organic Letters, 2012)

Efficient Substitution Reaction from Cysteine to the Serine Residue of Glycosylated Polypeptide: Repetitive Peptide Segment Ligation Strategy and the Synthesis of Glycosylated Tetracontapeptide Having Acid Labile Sialyl-T N Antigens - Okamoto, Ryo; Souma, Shingo; Kajihara, Yasuhiro (The Journal of Organic Chemistry, 2009)

Solid-Phase Synthesis of Peptide and Glycopeptide Thioesters through Side-Chain-Anchoring Strategies - Ficht, Simon; Payne, Richard J.; Guy, Richard T.; Wong, Chi-Huey (Chemistry - A European Journal, 2008)

Synthesis of lucifensin by native chemical ligation and characteristics of its isomer having different disulfide bridge pattern: SYNTHESIS OF LUCIFENSIN BY NATIVE CHEMICAL LIGATION - Stanchev, Stancho; Zawada, Zbigniew; Monincová, Lenka; Bednárová, Lucie; Slaninová, Jiřina; Fučík, Vladimír; Čeřovský, Václav (Journal of Peptide Science, 2014)

Efficient Substitution Reaction from Cysteine to the Serine Residue of Glycosylated Polypeptide: Repetitive Peptide Segment Ligation Strategy and the Synthesis of Glycosylated Tetracontapeptide Having Acid Labile Sialyl-T N Antigens - Okamoto, Ryo; Souma, Shingo; Kajihara, Yasuhiro (The Journal of Organic Chemistry, 2009)

An Orthogonal Double-Linker Resin Facilitates the Efficient Solid-Phase Synthesis of Complex-Type N-Glycopeptide Thioesters Suitable for Native Chemical Ligation - Mezzato, Stefano; Schaffrath, Manuela; Unverzagt, Carlo (Angewandte Chemie International Edition, 2005)

Synthesis of lucifensin by native chemical ligation and characteristics of its isomer having different disulfide bridge pattern: SYNTHESIS OF LUCIFENSIN BY NATIVE CHEMICAL LIGATION - Stanchev, Stancho; Zawada, Zbigniew; Monincová, Lenka; Bednárová, Lucie; Slaninová, Jiřina; Fučík, Vladimír; Čeřovský, Václav (Journal of Peptide Science, 2014)

Isolation of two insecticidal toxins from venom of the Australian theraphosid spider Coremiocnemis tropix - Ikonomopoulou, Maria P.; Smith, Jennifer J.; Herzig, Volker; Pineda, Sandy S.; Dziemborowicz, Sławomir; Er, Sing-Yan; Durek, Thomas; Gilchrist, John; Alewood, Paul F.; Nicholson, Graham M.; Bosmans, Frank; King, Glenn F. (Toxicon, 2016)

An Orthogonal Double-Linker Resin Facilitates the Efficient Solid-Phase Synthesis of Complex-Type N-Glycopeptide Thioesters Suitable for Native Chemical Ligation - Mezzato, Stefano; Schaffrath, Manuela; Unverzagt, Carlo (Angewandte Chemie International Edition, 2005)

Isolation of two insecticidal toxins from venom of the Australian theraphosid spider Coremiocnemis tropix - Ikonomopoulou, Maria P.; Smith, Jennifer J.; Herzig, Volker; Pineda, Sandy S.; Dziemborowicz, Sławomir; Er, Sing-Yan; Durek, Thomas; Gilchrist, John; Alewood, Paul F.; Nicholson, Graham M.; Bosmans, Frank; King, Glenn F. (Toxicon, 2016)

Isolation, synthesis and characterization of ω-TRTX-Cc1a, a novel tarantula venom peptide that selectively targets L-type CaV channels - Klint, Julie K.; Berecki, Géza; Durek, Thomas; Mobli, Mehdi; Knapp, Oliver; King, Glenn F.; Adams, David J.; Alewood, Paul F.; Rash, Lachlan D. (Biochemical Pharmacology, 2014)

Isolation, synthesis and characterization of ω-TRTX-Cc1a, a novel tarantula venom peptide that selectively targets L-type CaV channels - Klint, Julie K.; Berecki, Géza; Durek, Thomas; Mobli, Mehdi; Knapp, Oliver; King, Glenn F.; Adams, David J.; Alewood, Paul F.; Rash, Lachlan D. (Biochemical Pharmacology, 2014)

An Approach for a Synthesis of Asparagine-Linked Sialylglycopeptides Having Intact and Homogeneous Complex-Type Undecadisialyloligosaccharides - Yamamoto, Naoki; Takayanagi, Ayumi; Yoshino, Ayako; Sakakibara, Tohru; Kajihara, Yasuhiro (Chemistry - A European Journal, 2007)

An Approach for a Synthesis of Asparagine-Linked Sialylglycopeptides Having Intact and Homogeneous Complex-Type Undecadisialyloligosaccharides - Yamamoto, Naoki; Takayanagi, Ayumi; Yoshino, Ayako; Sakakibara, Tohru; Kajihara, Yasuhiro (Chemistry - A European Journal, 2007)

Total chemical synthesis and X-ray structure of kaliotoxin by racemic protein crystallography - Pentelute, Brad L.; Mandal, Kalyaneswar; Gates, Zachary P.; Sawaya, Michael R.; Yeates, Todd O.; Kent, Stephen B. H. (Chemical Communications, 2010)

Total chemical synthesis and X-ray structure of kaliotoxin by racemic protein crystallography - Pentelute, Brad L.; Mandal, Kalyaneswar; Gates, Zachary P.; Sawaya, Michael R.; Yeates, Todd O.; Kent, Stephen B. H. (Chemical Communications, 2010)

Chemoselective Peptide Ligation-Desulfurization at Aspartate - Thompson, Robert E.; Chan, Bun; Radom, Leo; Jolliffe, Katrina A.; Payne, Richard J. (Angewandte Chemie International Edition, 2013)

Chemoselective Peptide Ligation-Desulfurization at Aspartate - Thompson, Robert E.; Chan, Bun; Radom, Leo; Jolliffe, Katrina A.; Payne, Richard J. (Angewandte Chemie International Edition, 2013)

Chemical synthesis and evaluation of a backbone-cyclized minimized 2-helix Z-domain - Järver, Peter; Mikaelsson, Cecilia; Karlström, Amelie Eriksson (Journal of Peptide Science, 2011)

Chemical synthesis and evaluation of a backbone-cyclized minimized 2-helix Z-domain - Järver, Peter; Mikaelsson, Cecilia; Karlström, Amelie Eriksson (Journal of Peptide Science, 2011)

Selective Desulfurization of Cysteine in the Presence of Cys(Acm) in Polypeptides Obtained by Native Chemical Ligation - Pentelute, Brad L.; Kent, Stephen B. H. (Organic Letters, 2007)

Selective Desulfurization of Cysteine in the Presence of Cys(Acm) in Polypeptides Obtained by Native Chemical Ligation - Pentelute, Brad L.; Kent, Stephen B. H. (Organic Letters, 2007)

Synthesis of an iberiotoxin derivative by chemical ligation: A method for improved yields of cysteine-rich scorpion toxin peptides - Bingham, Jon-Paul; Chun, Joycelyn B.; Ruzicka, Margaret R.; Li, Qing X.; Tan, Zhi-Yong; Kaulin, Yuri A.; Englebretsen, Darren R.; Moczydlowski, Edward G. (Peptides, 2009)

Synthesis of an iberiotoxin derivative by chemical ligation: A method for improved yields of cysteine-rich scorpion toxin peptides - Bingham, Jon-Paul; Chun, Joycelyn B.; Ruzicka, Margaret R.; Li, Qing X.; Tan, Zhi-Yong; Kaulin, Yuri A.; Englebretsen, Darren R.; Moczydlowski, Edward G. (Peptides, 2009)

Synthesis of the Bacteriocin Glycopeptide Sublancin 168 and S -Glycosylated Variants - Hsieh, Yves S. Y.; Wilkinson, Brendan L.; O’Connell, Mitchell R.; Mackay, Joel P.; Matthews, Jacqueline M.; Payne, Richard J. (Organic Letters, 2012)

Synthesis of the Bacteriocin Glycopeptide Sublancin 168 and S -Glycosylated Variants - Hsieh, Yves S. Y.; Wilkinson, Brendan L.; O’Connell, Mitchell R.; Mackay, Joel P.; Matthews, Jacqueline M.; Payne, Richard J. (Organic Letters, 2012)

Examination of native chemical ligation using peptidyl prolyl thioesters - Nakamura, Takahiro; Shigenaga, Akira; Sato, Kohei; Tsuda, Yusuke; Sakamoto, Ken; Otaka, Akira (Chem. Commun., 2014)

Examination of native chemical ligation using peptidyl prolyl thioesters - Nakamura, Takahiro; Shigenaga, Akira; Sato, Kohei; Tsuda, Yusuke; Sakamoto, Ken; Otaka, Akira (Chem. Commun., 2014)