文献类型：期刊文献

英文题名：Silk Sericin-inspired Poly-β-homoserine for Protein Protection

作者：Zhang, Jun-Yu[1];Cai, Jia-Yi[1];Zhang, Dong-Hui[2];Liu, Long-Qiang[1];Zhi, Zhong-Hua[1];Li, Bing[1];Chen, Qi[1];Liu, Run-Hui[1,2,3]

机构：[1]East China Univ Sci & Technol, Shanghai Frontiers Sci Ctr Optogenet Tech Cell Met, Frontiers Sci Ctr Materiobiol & Dynam Chem, Sch Mat Sci & Engn,State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Chinese Acad Sci, Suzhou Inst Biomed Engn & Technol, Suzhou 215163, Peoples R China;[3]Fudan Univ, State Key Lab Mol Engn Polymers, Shanghai 200438, Peoples R China

年份：2026

外文期刊名：CHINESE JOURNAL OF POLYMER SCIENCE

收录：;EI(收录号：20262921138579);Scopus(收录号：2-s2.0-105044866277);WOS:【SCI-EXPANDED(收录号:WOS:001820578700001)】；

基金：This work was financially supported by the National Key R&D Program of China (No. 2024YFC2418700), the National Natural Science Foundation of China (Nos. T2325010, 52361165622 and 32301124), the Natural Science Foundation of Jiangsu Province (No. BK20243003), and the Shanghai Frontiers Science Center of Optogenetic Techniques for Cell Metabolism (Shanghai Municipal Education Commission).The authors thank the Research Center of Analysis and Test of East China University of Science and Technology for the help on the characterization for studies reviewed in this manuscript. The authors also thank the staff members of the Large-scale Protein Preparation System at the National Facility for Protein Science in Shanghai (NFPS), Zhangjiang Lab, China, for providing technical support and assistance in data collection and analysis.

语种：英文

外文关键词：Silk sericin; Poly-beta-homoserine; Protein protection; Stabilizer; Ring-opening polymerization

摘要：Protein stability is a critical factor that limits its application in biopharmaceuticals, clinical diagnostics, and industrial production. The inherent instability of proteins renders them susceptible to loss of activity and function under external environmental stresses, thus necessitating the development of novel stabilizers to improve protein stability. Inspired by sericin, we developed heterochiral poly-beta-homoserine (beta-HS) that combines resistance to enzymatic degradation, straightforward synthesis, and precise composition control, while exhibiting favorable in vitro safety profile. The beta-HS exhibits remarkable stabilizing effects on horseradish peroxidase (HRP) and beta-galactosidase (beta-Gal) when subjected to elevated temperature and lyophilization, respectively. Our research indicates that beta-HS stabilizes proteins by assisting in the maintenance of their conformation and preventing aggregation. Additionally, beta-HS demonstrates stabilizing effects on proteins with diverse physicochemical properties. Therefore, this study suggests that the beta-HS is a promising candidate for enhancing protein stability.