文献类型：期刊文献

英文题名：Influences of Polyphenols on the Properties of Crosslinked Acellular Fish Swim Bladders: Experiments and Molecular Dynamic Simulations

作者：Han, Yuqing[1];Jiang, Jie[1];Li, Jinjin[1];Zhao, Ling[1,2];Xi, Zhenhao[1,2]

机构：[1]East China Univ Sci & Technol, Sch Chem Engn, State Key Lab Chem Engn, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, Shanghai Key Lab Multiphase Mat Chem Engn, Shanghai 200237, Peoples R China

年份：2024

卷号：16

期号：8

外文期刊名：POLYMERS

收录：;EI(收录号：20241815998078);WOS:【SCI-EXPANDED(收录号:WOS:001210056200001)】；

基金：No Statement Available

语种：英文

外文关键词：polyphenols; acellular fish swim bladder; crosslinking; molecular dynamic simulation; enzymic stability

摘要：Acellular fish swim bladders (AFSBs) are a promising biomaterial in tissue engineering, however, they may suffer from rapid degradation due to enzyme invasion. In this work, natural polyphenols, including epigallocatechin gallate (EGCG), proanthocyanidin (PC), tannic acid (TA) and protocatechuic acid (PCA), were utilized to improve the properties of AFSBs through crosslinking modifications. Fourier transform infrared (FTIR) results indicate that the triple helix of the collagen in AFSBs is well preserved after crosslinking. The differential scanning calorimetry (DSC), water contact angle (WCA) and in vitro degradation tests indicate that the polyphenol-crosslinked AFSBs exhibit improved thermal stability, enzymatic stability, hydrophilicity and mechanical properties. Among them, EGCG with multiple phenolic hydroxyl groups and low potential resistance is more favorable for the improvement of the mechanical properties and enzymatic stability of AFSBs, as well as their biocompatibility and integrity with the collagen triple helix. Moreover, the crosslinking mechanism was demonstrated to be due to the hydrogen bonds between polyphenols and AFSBs, and was affected by the molecular size, molecular weight and the hydroxyl groups activity of polyphenol molecules, as clarified by molecular dynamic (MD) simulations. The approach presented in this work paves a path for improving the properties of collagen materials.