Synlett 2015; 26(03): 285-293
DOI: 10.1055/s-0034-1379946
synpacts
© Georg Thieme Verlag Stuttgart · New York

Synthesizing Clickable Glutathione by Glutathione Synthetase Mutant for Detecting Protein Glutathionylation

Kusal T. G. Samarasinghe
Wayne State University, Chemistry Building, Cass Avenue, Detroit, MI 48202, USA   Email: yahn@chem.wayne.edu
,
Young-Hoon Ahn*
Wayne State University, Chemistry Building, Cass Avenue, Detroit, MI 48202, USA   Email: yahn@chem.wayne.edu
› Author Affiliations
Further Information

Publication History

Received: 12 October 2014

Accepted after revision: 21 November 2014

Publication Date:
12 January 2015 (online)


Abstract

In response to reactive oxygen species (ROS), glutathione plays an important role in redox signaling by forming a disulfide bond with protein cysteine residues, known as glutathionylation. We briefly review the roles of glutathione, ROS, and glutathionylation in redox regulation. We then introduce common biochemical methods for identifying glutathionylation and highlight our recent chemical method for selective detection of glutathionylation. The merits, limitations, and future applications of our approach are also discussed.