Chem. J. Chinese Universities ›› 2000, Vol. 21 ›› Issue (2): 306.

• Articles • Previous Articles     Next Articles

Coordination Structure and Higher Order Structure of Cu(Ⅱ)-Silk Fibroin Protein(Bombyx Mori) Complexes

CHEN Wen-Xing1, SHEN Zhi-Quan2, LIU Guan-Feng1, SHIRAI Hirofusa3   

  1. 1. Collegeof Textile Science&Technology, Zhejiang Instituteof Science&Technology, Hangzhou 310033, China;
    2. Departmentof Polymer Science & Engineering, Zhejiang University, Hangzhou 310027, China;
    3. Facultyof Textile Science & Technology, Shinshu University, Ueda 386-8567, Japan
  • Received:1999-10-27 Online:2000-02-24 Published:2000-02-24

Abstract: The copper(Ⅱ) complexes of silk fibroin protein of Bombyx mori are prepared by homogeneous and heterogeneous phase coordination reaction at different pHvalues, and their coordination structures and aggregated structures are investigated by means of spectroscopy, electron spin resonance(ESR) and X-ray diffraction(XRD) measurements. Under the basic condition (pH=10.60), one type of complex is formed which contains four nitrogens from peptide main chain at the corners of a square in which the copper(Ⅱ) occupies the center, and while under the acid condition(pH=4.30, 5.88), other complex is obtained, which is mainly formed by the carboxyl of peptide side or end groups binding copper(Ⅱ) as Cu(Ⅱ)· (-COO-) (H2O)3and Cu(Ⅱ)(-COO-)2.The higher order structures of Cu(Ⅱ)-silk fibroin protein complexes prepared under various conditions are also discussed and described.

Key words: Silk fibroin protein, Copper(Ⅱ) complex, Coordination structure, Higher order structure

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