Semi-enzymatic acceleration of oxidative protein folding by <i>N</i>-methylated heteroaromatic thiols
Shunsuke Okada, Yosuke Matsumoto, Rikana Takahashi, Kenta Arai, Shingo Kanemura, Masaki Okumura, Takahiro Muraoka
Abstract
We report the first example of a synthetic thiol-based compound that promotes oxidative protein folding upon 1-equivalent loading to the disulfide bonds in the client protein to afford the native form in over 70% yield.
Topics & Concepts
ChemistryOxidative foldingFolding (DSP implementation)Protein foldingThiolMethylationOxidative phosphorylationDisulfide bondProtein disulfide-isomerasePosttranslational modificationCombinatorial chemistryEnzymeBiochemistryStereochemistryDNAEngineeringElectrical engineeringSignaling Pathways in DiseaseCancer-related gene regulationEndoplasmic Reticulum Stress and Disease