Enzymatic “Click” Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase
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Pentelute_Enzymatic.pdf
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Author(s)
Zhang, Chi
Spokoyny, Alexander M.
Zou, Yekui
Pentelute, Bradley L.
Simon, Mark
Date Issued
November 2013
Journal
Angewandte Chemie International Edition
Publisher
Wiley Blackwell
Citation
Zhang, Chi, Alexander M. Spokoyny, Yekui Zou, Mark D. Simon, and Bradley L. Pentelute. “Enzymatic ‘Click’ Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase.” Angewandte Chemie International Edition 52, no. 52 (November 12, 2013): 14001–14005.
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Author's final manuscript
Abstract
Singled out for special treatment: Naturally occurring glutathione S-transferase (GST) was used to catalyze an efficient “click” ligation between polypeptides with an N-terminal glutathione sequence and biomolecules or chemical probes containing perfluorinated aromatic groups (see scheme). The site-specific modification of one cysteine residue was possible in the presence of other unprotected cysteine residues and reactive functional groups.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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Creative Commons Attribution-Noncommercial-Share Alike
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DOI of Published Version
https://doi.org/10.1002/anie.201306430
