Chemical Research in Chinese Universities ›› 2017, Vol. 33 ›› Issue (2): 166-171.doi: 10.1007/s40242-017-6361-1

• Articles • Previous Articles     Next Articles

Fluorescence Spectroscopic Studies on the Interaction Between a New Bismuth(III) Schiff Base Complex and Bovine Serum Albumin

LI Xu1, LI Chuanhua1, JIANG Jianhong1, GU Huiwen2, WEI Deliang1, YE Lijuan1, HU Jilin1, XIAO Shengxiong1, ZHANG Hui1, LI Xia1, LI Qiangguo1   

  1. 1. Hunan Provincial Key Laboratory of Xiangnan Rare-precious Metals Compounds and Applications, College of Chemistry Biology and Environmental Engineering, Xiangnan University, Chenzhou 423043, P. R. China;
    2. College of Chemistry and Environmental Engineering, Yangtze University, Jingzhou 434023, P. R. China
  • Received:2016-08-30 Revised:2016-11-17 Online:2017-04-01 Published:2017-01-09
  • Contact: GU Huiwen,E-mail:gugo@yangtzeu.edu.cn;LI Qiangguo,E-mail:liqiangguo@163.com E-mail:gugo@yangtzeu.edu.cn;liqiangguo@163.com
  • Supported by:

    Supported by the National Natural Science Foundation of China(Nos.21273190, 20973145), the Science and Technology Plan Projects of Hunan Province, China(No.2014TT2026) and the Educational Committee Foundation of Hunan Province, China (Nos.15C1272, 15A175, 14A134).

Abstract:

In this work, the binding interaction between a new bismuth(III) Schiff base complex {[Bi(valen)]Cl·2H2O}[H2valen=N,N'-bis(2-hydroxy-3-methoxyphenylmethylidene)-2,6-pyridinediamine, C21H19N3O4] and bovine serum albumin(BSA) was studied via fluorescence quenching method. The static quenching constant KLB and some thermodynamic parameters(e.g., △Gθ, △Hθ and △Sθ) of the interaction were estimated. In particular, the binding site between the complex and BSA was explored by molecular docking. On the basis of the mechanism of Förster energy transfer, the binding distance between the bismuth(III) Schiff base complex and BSA(Trp.213) as well as the transfer efficiency was obtained. Furthermore, the effect of the bismuth(III) Schiff base complex on the conformation of BSA was investigated using synchronous fluorescence spectroscopy.

Key words: Bismuth(III) Schiff base complex, Bovine serum albumin, Fluorescence quenching, Molecular docking