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Clickable glutathione using tetrazine-alkene bioorthogonal chemistry for detecting protein glutathionylation
Journal article   Peer reviewed

Clickable glutathione using tetrazine-alkene bioorthogonal chemistry for detecting protein glutathionylation

Dilini N Kekulandara, Kusal T G Samarasinghe, Dhanushka N P Munkanatta Godage and Young-Hoon Ahn
Organic & biomolecular chemistry, v 14(46), pp 10886-10893
22 Nov 2016
DOI: https://doi.org/10.1039/c6ob02050j
PMID: 27812596
Featured in Collection :   UN Sustainable Development Goals @ Drexel

Abstract

Protein glutathionylation is one of the major cysteine oxidative modifications in response to reactive oxygen species (ROS). We recently developed a clickable glutathione approach for detecting glutathionylation by using a glutathione synthetase mutant (GS M4) that synthesizes azido-glutathione (γGlu-Cys-azido-Ala) in situ in cells. In order to demonstrate the versatility of clickable glutathione and to increase the chemical tools for detecting glutathionylation, we sought to develop clickable glutathione that uses tetrazine-alkene bioorthogonal chemistry. Here we report two alkene-containing glycine surrogates (allyl-Gly and allyl-Ser) for the biosynthesis of clickable glutathione and their use for detection, enrichment, and identification of glutathionylated proteins. Our results provide chemical tools (allyl-Gly and allyl-Ser for GS M4) for versatile characterization of protein glutathionylation. In addition, we show that the active site of GS can be tuned to introduce a small size chemical tag on glutathione for exploring glutathione function in cells.

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22 citations in Web of Science
22 citations in Scopus

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UN Sustainable Development Goals (SDGs)

This publication has contributed to the advancement of the following goals:

#3 Good Health and Well-Being

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Web of Science research areas
Chemistry, Organic
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