文献类型：期刊文献

英文题名：The Cheap Silk Sericin Displaying Chaperone-Like Activity to Stabilize Protein and Facilitate Protein Refolding

作者：Zhang, Junyu[1,2,3];Xiao, Xingqing[4];Zhang, Donghui[1];Liu, Longqiang[1,2];Zhang, Wenjing[5];Liang, Qian[1,2];Liu, Runhui[1,2,3]

机构：[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, Shanghai Frontiers Sci Ctr Optogenet Tech Cell Met, Frontiers Sci Ctr Materiobiol & Dynam Chem,Key Lab, Engn Res Ctr Biomed Mat,Minist Educ,Sch Mat Sci &, Shanghai 200237, Peoples R China;[3]Chinese Acad Sci, Suzhou Inst Biomed Engn & Technol, Suzhou 215163, Peoples R China;[4]Hainan Univ, Sch Chem & Chem Engn, Dept Chem, Haikou 570228, Hainan, Peoples R China;[5]Shanghai Jiao Tong Univ, Shanghai Gen Hosp, Dept Orthoped Surg, Sch Med, Shanghai 200080, Peoples R China

年份：2025

卷号：7

期号：7

起止页码：2185

外文期刊名：CCS CHEMISTRY

收录：WOS:【ESCI(收录号:WOS:001511002500001)】；

基金：This research was supported by the National Natural Science Foundation of China (grant nos. T2325010 and 52361165622) , Shanghai Frontiers Science Center of Optogenetic Techniques for Cell Metabolism (Shanghai Municipal Education Commission) , the Fundamental Research Funds for the Central Universities (grant nos. JKVD1241029 and JKD01241701) , the Open Research Fund of State Key Laboratory of Polymer Physics and Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences.

语种：英文

外文关键词：tein stabilization; environmental stress; molecular; dynamics simulation; silk sericin; chaperone-like activity; protein stabilization

摘要：The inherent instability of proteins limits their application, which urgently calls for protein stabilizers to protect proteins from various environmental stresses. Inspired by late embryogenesis abundant proteins, we found that sericin exhibits chaperone-like activity and effectively stabilizes proteins. Sericin exhibits exceptional stabilization of horseradish peroxidase (HRP) under heat stress, mechanical force, acidic conditions, organic solvents, and lyophilization, facilitating the refolding of denatured HRP because of the interactions with proteins through van der Waals forces and electrostatic interactions. The protein stabilizing function of sericin is widely applicable to proteins with different physicochemical properties such as beta-galactosidase, glucose oxidase, and antibody under various environmental stresses. Moreover, the easily accessible sericin has excellent biocompatibility as a natural protein and cheap cost as discarded natural resource. These suggest the great potential of sericin as an efficient protein stabilizer to display chaperone-like activities.