A covalently crosslinked silk fibroin hydrogel using enzymatic oxidation and chemoenzymatically synthesized copolypeptide crosslinkers consisting of a GPG tripeptide motif and tyrosine: control of gelation and resilience

文献信息

发布日期 2020-04-08

DOI 10.1039/D0PY00187B

影响因子 5.582

作者

Hiromitsu Sogawa, Takuya Katashima, Keiji Numata

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摘要

A covalently crosslinked silk fibroin hydrogel (ChemSF) was successfully formed via an enzymatic crosslinking reaction using chemoenzymatically synthesized copolypeptides [poly(GPGn-r-Ym)], which consist of a glycine–proline–glycine (GPG) tripeptide motif and tyrosine (Y), as linker molecules. The gelation time of ChemSF was effectively shortened to less than 100 seconds without loss of toughness by adding poly(GPGn-r-Ym). In addition, the resilience of ChemSF was improved up to 86% at 66% strain, comparable to that of elastin, due to the flexible conformation of the poly(GPGn-r-Ym) crosslinker. The acceleration of the gelation and the improvement of the resilience of ChemSF were simultaneously achieved by using a multifunctional peptide crosslinker.

期刊推荐

Journal of the Royal Society of New Zealand

Chemical Society Reviews

Composites Science and Technology

Chemical Papers

Applied Organometallic Chemistry

Ceramics International

Bulletin of the Korean Chemical Society

Composite Structures

Heterocycles

Fire Safety Journal

来源期刊

Polymer Chemistry

CiteScore: 8.6

自引率: 7.3%

年发文量: 457

Polymer Chemistry welcomes submissions in all areas of polymer science that have a strong focus on macromolecular chemistry. Manuscripts may cover a broad range of fields, yet no direct application focus is required.

A covalently crosslinked silk fibroin hydrogel using enzymatic oxidation and chemoenzymatically synthesized copolypeptide crosslinkers consisting of a GPG tripeptide motif and tyrosine: control of gelation and resilience

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期刊推荐

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