Silk Sericin-inspired Poly-<italic style="font-style: italic">β</italic>-homoserine for Protein Protection

Jun-Yu Zhang; Jia-Yi Cai; Dong-Hui Zhang; Long-Qiang Liu; Zhong-Hua Zhi; Bing Li; Qi Chen; Run-Hui Liu

doi:10.1007/s10118-026-3691-9

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Silk Sericin-inspired Poly-β-homoserine for Protein Protection

RESEARCH ARTICLE | Updated：2026-07-10

- Silk Sericin-inspired Poly-β-homoserine for Protein Protection
- Silk Sericin-inspired Poly-β-homoserine for Protein Protection
- Chinese Journal of Polymer Science 2026年44卷页码：1-9
- Affiliations：
  
  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
- Author bio：
  
  rliu@ecust.edu.cn
- Funds：
  
  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.;The authors declare no interest conflict.Electronic supplementary information (ESI) is available free of charge in the online version of this article at http://doi.org/10.1007/s10118-026-3691-9.The data that support the findings of this study are available from the corresponding author upon reasonable request.
- DOI：10.1007/s10118-026-3691-9
  中图分类号：
- 收稿：2026-03-15，
  
  录用：2026-03-30，
  
  网络首发：2026-07-10，
  
  纸质出版：2026-05
- Accepted：
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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-β-homoserine for Protein Protection[J/OL]. Chinese Journal of Polymer Science, 2026, 441-9. DOI: 10.1007/s10118-026-3691-9.
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-β-homoserine for Protein Protection[J/OL]. Chinese Journal of Polymer Science, 2026, 441-9. DOI: 10.1007/s10118-026-3691-9. DOI：

摘要

Abstract

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-

-homoserine (

-HS) that combines resistance to enzymatic degradation

straightforward synthesis

and precise composition control

while exhibiting favorable in vitro safety profile. The

-HS exhibits remarkable stabilizing effects on horseradish peroxidase (HRP) and

-galactosidase (

-Gal) when subjected to elevated temperature and lyophilization

respectively. Our research indicates that

-HS stabilizes proteins by assisting in the maintenance of their conformation and preventing aggregation. Additionally

-HS demonstrates stabilizing effects on proteins with diverse physicochemical properties. Therefore

this study suggests that the

-HS is a promising candidate for enhancing protein stability.

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Keywords

references

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Silk Sericin-inspired Poly-β-homoserine for Protein Protection

Silk Sericin-inspired Poly-β-homoserine for Protein Protection

DOI：10.1007/s10118-026-3691-9

摘要

Abstract

关键词

Keywords

references