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再生丝素蛋白水溶液的流动稳定性研究

A study on the flow stability of regenerated silk fibroin aqueous solution.

作者信息

Wang Hong, Zhang Yaopeng, Shao Huili, Hu Xuechao

机构信息

State Key Laboratory for Modification of Chemical Fibers and Polymer Materials, College of Material Science and Engineering, Donghua University, Shanghai 200051, PR China.

出版信息

Int J Biol Macromol. 2005 Jul;36(1-2):66-70. doi: 10.1016/j.ijbiomac.2005.03.011.

DOI:10.1016/j.ijbiomac.2005.03.011
PMID:15916801
Abstract

The flow stability of silk fibroin (SF) aqueous solutions with different concentrations under different temperatures was investigated. It was found that the flow stability decreased quickly with the increase of solution concentration and temperature. X-ray diffraction, Fourier transform infrared (FTIR) and Raman spectroscopy analysis showed that silk fibroin in aqueous solution was mainly in random coil and alpha-helix conformation. However, it turned into alpha-helix and beta-sheet conformation after gelation, and both silk I and silk II crystalline structures appeared accordingly. The investigation implies that the original dilute regenerated SF aqueous solution should be stored under low temperature and concentrated just before spinning.

摘要

研究了不同浓度的丝素蛋白(SF)水溶液在不同温度下的流动稳定性。发现随着溶液浓度和温度的升高,流动稳定性迅速下降。X射线衍射、傅里叶变换红外(FTIR)和拉曼光谱分析表明,水溶液中的丝素蛋白主要呈无规卷曲和α-螺旋构象。然而,凝胶化后转变为α-螺旋和β-折叠构象,相应地出现了丝I和丝II晶体结构。该研究表明,原始的稀再生SF水溶液应低温储存,并在纺丝前进行浓缩。

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