金属离子导致的丝素蛋白的构象转变  

The Effect of Metal Ions on the Conformation Transition of Silk Fibroin

作　　者：李贵阳[1] 周平[1] 孙尧俊[2] 姚文华[2] 宓泳[1] YAO Hui-ying 姚惠英[1] 邵正中[1] 于同隐[1] 

机构地区：[1]复旦大学 [2]复旦大学分析测试中心, [3]Key Laboratory of Applied Ion Beam Physics,Ministry of Education, Fudan University,,上海200433

出　　处：《高等学校化学学报》2001年第5期860-862,共3页Chemical Journal of Chinese Universities

基　　金：国家自然科学基金! (批准号 :2 99740 0 4);教育部青年骨干基金;上海市自然科学基金! (批准号 :99ZA14 0 0 1;波谱与原子分子物

摘　　要：How the silkworm spins out such an excellent silk fiber has been a hot topic. The issue here is to know how the coil chains in the gland of silkworm transform to β sheet in silk fiber. We used the regenerated silk fibroin to imitate the silk fibroin of the gland to investigate the effect of metal ion(Ca 2+ . Cu 2+ ) on the silk spinning process of Bombyx mori silkworm. The solutions or gel obtained from hte mixture of regenerated silk fibroin and metal ions were dried for mimicking the gradual loss of water in the spinning process. The 13 C NMR spectrum simulation for C β nucleus of alanine quantitatively demonstrated that the conformation of the regenerated silk fibroin is dominantly of silk Ⅰ, whereas the fibroin with metal ions has more silk Ⅱ conformation. Raman spectroscopies show the consistent results with that of NMR. The binding of metal ion with carbonyl and amide in protein backbone allows the protein chain to array regularly, therefore leading to the β sheet formation.How the silkworm spins out such an excellent silk fiber has been a hot topic. The issue here is to know how the coil chains in the gland of silkworm transform to β sheet in silk fiber. We used the regenerated silk fibroin to imitate the silk fibroin of the gland to investigate the effect of metal ion(Ca 2+ . Cu 2+ ) on the silk spinning process of Bombyx mori silkworm. The solutions or gel obtained from hte mixture of regenerated silk fibroin and metal ions were dried for mimicking the gradual loss of water in the spinning process. The 13 C NMR spectrum simulation for C β nucleus of alanine quantitatively demonstrated that the conformation of the regenerated silk fibroin is dominantly of silk Ⅰ, whereas the fibroin with metal ions has more silk Ⅱ conformation. Raman spectroscopies show the consistent results with that of NMR. The binding of metal ion with carbonyl and amide in protein backbone allows the protein chain to array regularly, therefore leading to the β sheet formation.

关 键 词：丝素蛋白 构象转变 金属离子 核磁共振 

分 类 号：Q51[生物学—生物化学]