Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3 Aramaki-Aza-Aoba, Aoba-ku, Sendai, Miyagi, 980-8578, Japan.
Department of Molecular and Chemical Life Sciences, Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi, 980-8577, Japan.
Chem Commun (Camb). 2024 Jun 11;60(48):6134-6137. doi: 10.1039/d4cc01712a.
Compounds harboring high acidity and oxidizability of thiol groups permit tuning the redox equilibrium constants of CxxC sites of members of the protein disulphide isomerase (PDI) family and thus can be used to accelerate folding processes and increase the production of native proteins by minimal loading in comparison to glutathione.
含有高酸度和巯基氧化还原基团的化合物允许调节蛋白质二硫键异构酶(PDI)家族成员的 CxxC 位点的氧化还原平衡常数,因此与谷胱甘肽相比,可以通过最小负载加速折叠过程并增加天然蛋白质的产量。