Enzymatic "Click" Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase

• Main Authors: Zhang, Chi (Contributor), Spokoyny, Alexander M. (Contributor), Zou, Yekui (Contributor), Pentelute, Bradley L. (Contributor), Simon, Mark (Contributor)
• Other Authors: Massachusetts Institute of Technology. Department of Chemistry (Contributor)
• Format: Article
• Language: English
• Published: Wiley Blackwell, 2015-02-25T20:15:29Z.
• Subjects: Article
• Online Access: Get fulltext

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.
National Institutes of Health (U.S.) (GM101762)
National Institutes of Health (U.S.) (Award GM46059)
MIT Faculty Start-up Fund
Damon Runyon Cancer Research Foundation
Amgen Inc. (Summer Graduate Research Fellowship)