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

Zhang, J.; Sui, P.; Yang, W.; Shirshin, E.A.; Zheng, M.; Wei, B.; Xu, C.; Wang, H.

Статья опубликована в высокорейтинговом журнале

Информация о цитировании статьи получена из Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 20 февраля 2024 г.

Авторы: Zhang Juntao, Sui Peishan, Yang Wendian, Shirshin Evgeny A., Zheng Mingming, Wei Benmei, Xu Chengzhi, Wang Haibo
Журнал: International Journal of Biological Macromolecules
Том: 225
Год издания: 2023
Издательство: Elsevier BV
Местоположение издательства: Netherlands
Первая страница: 310
Последняя страница: 317
DOI: 10.1016/j.ijbiomac.2022.11.035
Аннотация: 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 α-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 α-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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Site-specific modification of N-terminal α-amino groups of succinylated collagenстатья

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