文献类型：期刊文献

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

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

机构：[1]State Key Laboratory of Bioreactor Engineering,East China University of Science and Technology,Shanghai 200237;[2]Shanghai Frontiers Science Center of Optogenetic Techniques for Cell Metabolism,Key Laboratory for Ultrafine Materials of Ministry of Education,Frontiers Science Center for Materiobiology and Dynamic Chemistry,Engineering Research Center for Biomedical Materials of Ministry of Education,School of Materials Science and Engineering,East China University of Science and Technology,Shanghai 200237;[3]Suzhou Institute of Biomedical Engineering and Technology,Chinese Academy of Sciences,Suzhou 215163;[4]Department of Chemistry,School of Chemistry and Chemical Engineering,Hainan University,Haikou City,Hainan Province 570228;[5]Department of Orthopedic Surgery,Shanghai General Hospital,Shanghai Jiao Tong University School of Medicine,Shanghai 200080

年份：2025

卷号：7

期号：7

起止页码：2185

中文期刊名：CCS Chemistry

外文期刊名：中国化学会会刊(英文)

基金：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

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

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 asβ-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.