

FOLLOWUS
a.State Key Laboratory of Bioreactor Engineering, Shanghai Frontiers Science Center of Optogenetic Techniques for Cell Metabolism, Frontiers Science Center for Materiobiology and Dynamic Chemistry, Key Laboratory for Ultrafine Materials of Ministry of Education, School of Materials Science and Engineering, East China University of Science and Technology, Shanghai 200237, China
b.Suzhou Institute of Biomedical Engineering and Technology, Chinese Academy of Sciences, Suzhou 215163, China
c.State Key Laboratory of Molecular Engineering of Polymers, Fudan University, Shanghai 200438, China
rliu@ecust.edu.cn
Received:15 March 2026,
Accepted:30 March 2026,
Online First:10 July 2026,
Published:2026-05
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Zhang, J. Y.; Cai, J. Y.; Zhang, D. H.; Liu, L. Q.; Zhi, Z. H.; Li, B.; Chen, Q.; Liu, R. H. Silk sericin-inspired poly-β-homoserine for protein protection. Chinese J. Polym. Sci. https://doi.org/10.1007/s10118-026-3691-9
Jun-Yu Zhang, Jia-Yi Cai, Dong-Hui Zhang, et al. Silk Sericin-inspired Poly-
Zhang, J. Y.; Cai, J. Y.; Zhang, D. H.; Liu, L. Q.; Zhi, Z. H.; Li, B.; Chen, Q.; Liu, R. H. Silk sericin-inspired poly-β-homoserine for protein protection. Chinese J. Polym. Sci. https://doi.org/10.1007/s10118-026-3691-9 DOI:
Jun-Yu Zhang, Jia-Yi Cai, Dong-Hui Zhang, et al. Silk Sericin-inspired Poly-
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-
β
-homoserine (
β
-HS) that combines resistance to enzymatic degradation
straightforward synthesis
and precise composition control
while exhibiting favorable in vitro safety profile. The
β
-HS exhibits remarkable stabilizing effects on horseradish peroxidase (HRP) and
β
-galactosidase (
β
-Gal) when subjected to elevated temperature and lyophilization
respectively. Our research indicates that
β
-HS stabilizes proteins by assisting in the maintenance of their conformation and preventing aggregation. Additionally
β
-HS demonstrates stabilizing effects on proteins with diverse physicochemical properties. Therefore
this study suggests that the
β
-HS is a promising candidate for enhancing protein stability.
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