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

被引：65

作者：

Zhang, Chi ^{[1
]}

Spokoyny, Alexander M. ^{[1
]}

Zou, Yekui ^{[1
]}

Simon, Mark D. ^{[1
]}

Pentelute, Bradley L. ^{[1
]}

机构：

[1] MIT, Dept Chem, Cambridge, MA 02139 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2013年 / 52卷 / 52期

基金：

美国国家卫生研究院;

关键词：

bioconjugation; click chemistry; cysteine arylation; enzyme catalysis; peptide macrocyclization; NATIVE CHEMICAL LIGATION; CELL-SURFACE PROTEINS; POSTTRANSLATIONAL MODIFICATIONS; CHEMISTRY; SITE; PEPTIDE; DESULFURIZATION; BIOCONJUGATION; STRATEGIES; VERSATILE;

D O I：

10.1002/anie.201306430

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：14001 / 14005

页数：5

共 67 条

[1] THE GLUTATHIONE-BINDING SITE IN GLUTATHIONE S-TRANSFERASES - INVESTIGATION OF THE CYSTEINYL, GLYCYL AND GAMMA-GLUTAMYL DOMAINS [J].