蚕丝蛋白与类动物丝蛋白聚合物共混膜的振动光谱研究

作     者：姚晋荣 陈新 周平 邵正中 于同隐 

作者机构：复旦大学高分子科学系聚合物分子工程教育部重点实验室上海200433 

出 版 物：《高等学校化学学报》 (Chemical Journal of Chinese Universities)

年 卷 期：2003年第24卷第11期

页      面：2113-2115页

核心收录：

学科分类：081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070303[理学-有机化学] 0703[理学-化学] 0803[工学-光学工程] 

基　　金：国家自然科学基金 (批准号 :2 0 2 44 0 0 5 ) 教育部高等学校博士学科点专项科研基金资助 

主　　题：蚕丝蛋白 类动物丝蛋白聚合物 共混膜 振动光谱 构象 

摘      要：Vibrational spectroscopy(ATR-FTIR and Raman) was used to investigate the interaction and conformation transition in the blend films of silk fibroin(SF) and silk-protein like polymers(P1, P2) containing the oligopeptide segments[(Ala) 4, GlyAlaGlyAla] which derived from the crystal region of spider dragline silk and silkworm(Bombyx mori) silk. The results revealed that the intermolecular hydrogen-bond interaction, which was formed between the molecular chains of SF and the oligopeptide segments in P1 and P2, induced a partial random coil/α-helix conformation transfer to β-sheet conformation after blending. And β-sheet and random coil/α-helix conformation coexisted in the SF/P1 and SF/P2 blend films, while the predominant conformations in the pure SF and P1 films were random coil/α-helix. These conclusions would be significant for artificial spinning of the regenerated silk fibroin.