Acta Chimica Sinica ›› 2007, Vol. 65 ›› Issue (19): 2197-2201. Previous Articles    

Original Articles

铁和锰对桑蚕丝蛋白构象转变的影响

周文1, 黄郁芳2, 邵正中1, 陈新*,1   

  1. (1复旦大学高分子科学系 教育部聚合物分子工程重点实验室 上海 200433)
    (2复旦大学材料科学系 国家微分析中心 上海 200433)
  • 投稿日期:2007-03-29 修回日期:2007-05-19 发布日期:2007-10-14
  • 通讯作者: 陈新

Effect of Fe and Mn on the Conformation Transition of Bombyx mori Silk Fibroin

ZHOU Wen1; HUANG Yu-Fang2; SHAO Zheng-Zhong1; CHEN Xin*,1   

  1. (1 The Key Laboratory of Molecular Engineering of Polymers of the Ministry of Education of China, Department of Macromolecular Science, Fudan University, Shanghai 200433)
    (2 National Microanalysis Center, Department of Material Science, Fudan University, Shanghai 200433)
  • Received:2007-03-29 Revised:2007-05-19 Published:2007-10-14
  • Contact: CHEN Xin

Inductively coupled plasma mass spectroscopy (ICP-MS) and atomic adsorption spectroscopy (AAS) were applied to determine the Fe and Mn contents in both silk glands and cocoon silks of Bombyx mori silkworms. In the meantime, Raman spectroscopy was used to monitor the effect of Fe(III) and Mn(II) on the conformation changes of silk protein in the concentrated regenerated silk fibroin solutions. The results showed that the Fe content in cocoon silk was higher than that in the silk gland, but the Mn content was on the other way round. In addition, the Fe content was gradually increased from the posterior part to the ante-rior part of the silk gland. However, the Mn content did not exhibit the same tendency as Fe did but showed the lowest value in the middle part of the silk gland. Finally the Raman spectra indicated that Fe(III) was able to induce the conformation transition of silk fibroin from random coil and/or helix conformation to β-sheet but Mn(II) seemed no such an effect.

Key words: metal element, concentrated regenerated silk fibroin solution, Raman spectroscopy, conformation transition, spinning mechanism, tyrosine