Work

Enzymatic “Click” Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S‐Transferase

Year: 2013

Type: article

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.

Source: Angewandte Chemie International Edition

DOI: 10.1002/anie.201306430

Authors: Chi Zhang, Alexander M. Spokoyny, Yekui Zou, Mark D. Simon, Bradley L. Pentelute

Institution: Massachusetts Institute of Technology

Language: English

Topic: Click Chemistry and Applications

Subfield: Organic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Awards: G1483833782, G4317863024, CATALYTIC METHODS FOR ORGANIC SYNTHESIS, Metal Catalyzed CN and CS Bond Forming Reactions for Bioconjugation Targets, Catalytic Methods for Organic Synthesis