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Evaluation of a dithiocarbamate derivative as an inhibitor of human glutaredoxin-1
Journal article   Peer reviewed

Evaluation of a dithiocarbamate derivative as an inhibitor of human glutaredoxin-1

S.S. Sadhu, E. Callegari, Y. Zhao, X. Guan and T. Seefeldt
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol.28(3), pp.456-462
2013
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Abstract

Context: Glutaredoxins (GRX) are involved in the regulation of thiol redox state. GRX-1 is a cytosolic enzyme responsible for the catalysis of deglutathionylation of proteins. To date, very few inhibitors of GRX-1 have been reported. Objective: The objective of this paper is to report 2-acetylamino-3-[4-(2-acetylamino-2-carboxyethyl-sulfanylthiocarbonylamino)phenylthiocarbamoylsulfanyl]propionic acid (2-AAPA) as an inhibitor of human GRX-1. Materials and methods: The mechanism of inhibition of GRX-1 was investigated using dialysis, substrate protection, and mass spectrometry. Results: 2-AAPA inhibits GRX-1 in a time and concentration dependent manner. The activity did not return following dialysis indicating that inhibition is irreversible. Results of substrate protection and mass spectrometry indicate that the inhibition is occurring at the active site. The compound also produced GRX inhibition in human ovarian cancer cells. Discussion: 2-AAPA is an irreversible GRX-1 inhibitor with similar or greater potency compared to previously reported inhibitors. Conclusion: The inhibition of GRX-1 by 2-AAPA could be used as a tool to study thiol redox state.

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Collaboration types
Domestic collaboration
Citation topics
1 Clinical & Life Sciences
1.127 Molecular & Cell Biology - Pharmacology
1.127.973 Thiol-Disulfide Systems
Web Of Science research areas
Biochemistry & Molecular Biology
Chemistry, Medicinal
ESI research areas
Biology & Biochemistry
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