蚕丝蛋白与类动物丝蛋白聚合物共混膜的振动光谱研究

蚕丝纤维具有优良的力学性能 ,不同的环境条件对其力学性能有一定的影响 ,但其力学性能主要取决于形成纤维过程中所形成的以分子链 β-折叠结构及其沿纤维轴方向高度取向为特征的丝纤维凝聚态结构 [1,2 ] .因此在丝纤维的形成及丝蛋白膜的人工制备过程中 ,丝蛋白分子链的构象及其构象转变一直是研究的重点[3～ 6 ] .以蚕丝蛋白 (Silk Fibroin,SF)稀溶液在常温下浇铸的 SF膜一般以无规线团 /α-螺旋为主的构象状态存在 ;经热处理、极性溶剂 (如甲醇等 )处理、应力作用或共混入一些能与SF形成分子间氢键的聚合物组分后 ,SF膜的构象将从无…

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

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.