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

• DOI: 10.1002/cbic.201700624
• Publication Date: 2017-12-02T06:36:38Z
• Authors: Kenta Arai; Haruhito Ueno; Yuki Asano; Gaurango Chakrabarty; Shingo Shimodaira; Govindasamy Mugesh; Michio Iwaoka
• Keywords: Foldase; Folding (DSP implementation); Oxidative folding; Cleavage (geology); Chemical chaperone

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