Enzymatic “Click” Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase
Author(s)Zhang, Chi; Spokoyny, Alexander M.; Zou, Yekui; Pentelute, Bradley L.; Simon, Mark
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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.
DepartmentMassachusetts Institute of Technology. Department of Chemistry
Angewandte Chemie International Edition
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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