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

Abstract

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

CLC Number:

O631

TrendMD:

YAO Jin-Rong, CHEN Xin, ZHOU Ping, SHAO Zheng-Zhong, YU Tong-Yin . Vibrational Spectroscopy Studies on the Blend Films of Silk Fibroin and Silk-protein Like Polymers[J]. Chem. J. Chinese Universities, 2003, 24(11): 2113.

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

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