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Protein Folding in the Presence of Water-Soluble Cyclic Diselenides with Novel Oxidoreductase and Isomerase Activities

Arai, Kenta and Ueno, Haruhito and Asano, Yuki and Chakrabarty, Gaurango and Shimodaira, Shingo and Mugesh, Govindasamy and Iwaoka, Michio (2018) Protein Folding in the Presence of Water-Soluble Cyclic Diselenides with Novel Oxidoreductase and Isomerase Activities. In: CHEMBIOCHEM, 19 (3). pp. 207-211.

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Official URL: http://dx.doi.org/10.1002/cbic.201700624

Abstract

The protein disulfide isomerase (PDI) family, found in the endoplasmic reticulum (ER) of the eukaryotic cell, catalyzes the formation and cleavage of disulfide bonds and thereby helps in protein folding. A decrease in PDI activity under ER stress conditions leads to protein misfolding, which is responsible for the progression of various human diseases, such as Alzheimer's, Parkinson's, diabetes mellitus, and atherosclerosis. Here we report that water-soluble cyclic diselenides mimic the multifunctional activity of the PDI family by facilitating oxidative folding, disulfide formation/reduction, and repair of the scrambled disulfide bonds in misfolded proteins.

Item Type: Journal Article
Additional Information: Copy right for this article belong to the WILEY-V C H VERLAG GMBH, POSTFACH 101161, 69451 WEINHEIM, GERMANY
Department/Centre: Division of Chemical Sciences > Inorganic & Physical Chemistry
Depositing User: Id for Latest eprints
Date Deposited: 02 Mar 2018 14:56
Last Modified: 02 Mar 2018 14:56
URI: http://eprints.iisc.ac.in/id/eprint/59042

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