自愈水凝胶
无定形固体
材料科学
聚合物
生物相容性
纳米技术
丝素
高分子
分子间力
分子
丝绸
化学工程
复合材料
结晶学
化学
高分子化学
有机化学
生物化学
工程类
冶金
作者
Yu Fu,Qinrui Lin,Rui Lan,Zhengzhong Shao
出处
期刊:Small
[Wiley]
日期:2024-09-02
标识
DOI:10.1002/smll.202403376
摘要
Proteins are classified as biopolymers which share similar structural features with semi-crystalline polymers. Although their unique biocompatibility facilitates the universal applications of protein-based hydrogels in the biomedical field, the mechanical performances of protein-based hydrogels fall short of practical requirements. Conventional strategies for enhancing mechanical properties focus on forming regularly folded secondary structures as analogs of crystalline regions. This concept is based on proteins as the analogy of semi-crystalline polymers, in which crystalline regions profoundly contribute to the mechanical performances. Even though the contribution of the amorphous region is equally weighted for semi-crystalline polymers, their capacity to improve the mechanical performances of protein-based structures is still undervalued. Herein, the potential of promoting the mechanical performances is explored by controlling the state of amorphous regions in protein-based hydrogels. A fibril protein is chosen, regenerated silk fibroin (RSF), as a model molecule for its similar viscoelasticity with a semi-crystalline polymer. The amorphous regions in the RSF hydrogels are transformed from extended to entangled states through a double-crosslinking method. The formation of entanglement integrates new physically crosslinked points for remarkable improvement in mechanical performances. A robust hydrogel is not only developed but also intended to provide new insights into the structural-property relationship of protein-based hydrogels.
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