高等学校化学学报 ›› 2003, Vol. 24 ›› Issue (11): 2113.

• 研究快报 • 上一篇    下一篇

蚕丝蛋白与类动物丝蛋白聚合物共混膜的振动光谱研究

姚晋荣, 陈新, 周平, 邵正中, 于同隐   

  1. 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
  • 收稿日期:2003-06-02 出版日期:2003-11-24 发布日期:2003-11-24
  • 通讯作者: 邵正中(1964年出生),男,博士,教授,博士生导师,主要从事生物大分子研究.E-mail:zzshao@fudan.edu.cn E-mail:zzshao@fudan.edu.cn
  • 基金资助:

    国家自然科学基金(批准号:20244005);教育部高等学校博士学科点专项科研基金资助

Vibrational Spectroscopy Studies on the Blend Films of Silk Fibroin and Silk-protein Like Polymers

YAO Jin-Rong, CHEN Xin, ZHOU Ping, SHAO Zheng-Zhong, YU Tong-Yin   

  1. Department of Macromolecular Science, Key Laboratory of Molecular Engineering of Polymers of State Educational Ministry, Fudan University, Shanghai 200433, China
  • Received:2003-06-02 Online:2003-11-24 Published:2003-11-24

关键词: 蚕丝蛋白, 类动物丝蛋白聚合物, 共混, 振动光谱

Abstract: 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 segmentSIn 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 conformationSIn the pure SFand P1 films were random coil/α-helix.These conclusions would be significant for artificial spinning of the regenerated silk fibroin.

Key words: Silk fibroin, Silk-protein like polymer, Blend, Vibrational spectroscopy

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