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 oligopeptid...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.展开更多
基金Hongtao Bian acknowledges the support from the National Natural Science Foundation of China(No.22173054)Hongtao Bian also thanks the financial support from Fundamental Research Funds for the Central Universities(GK202001009)+2 种基金Natural Science Fundamental Research Plan of Shaanxi Province(No.2024JC-JCQN-15)111 Project(B14041)Program for Changjiang Scholars and the Innovative Research Team in University(IRT-14R33).
文摘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.