Site-specific modification of N-terminal alpha-amino groups of succinylated collagen

文献类型： 外文期刊

第一作者： Zhang, Juntao

作者： Zhang, Juntao;Sui, Peishan;Yang, Wendian;Zheng, Mingming;Wei, Benmei;Xu, Chengzhi;Wang, Haibo;Shirshin, Evgeny A.;Zheng, Mingming

作者机构：

关键词： Succinylated collagen; Site -specific modification; PNIPAAm

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.2； 五年影响因子：7.8 ）

ISSN： 0141-8130

年卷期： 2023 年 225 卷

页码：

收录情况： SCI

摘要： Polymer based protein engineering provides an attractive strategy to endow novel properties to protein and overcome the inherent limitations of both counterparts. The exquisite control of site and density of attached polymers on the proteins is crucial for the bioactivities and properties of the protein-polymer bioconjugates, but is still a challenge. Collagen is the major structural protein in extracellular matrix of animals. Based on the advancements of polymer-based protein engineering, collagen bioconjugates has been widely fabricated and applied as biomaterials. However, the site-specific synthesis of well-defined collagen-polymer bioconjugates is still not achieved. Herein, a versatile strategy for the specific modification of N-terminal alpha-amino groups in collagen was developed. Firstly, all reactive amino groups of tropocollagen (collagen with telopeptides) were protected by succinic anhydride. Then, the telopeptides were digested to give the active N-terminal alpha-amino groups, which were subsequently attached with poly(N-isopropylacrylamide) (PNIPAAm) via "grafting from" method based on the atom transfer radical polymerization (ATRP). The site-specific N-terminal PNIPAAm modified succinylated collagen was prepared and its structure, thermal responsive behaviour, and properties was explored.

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