SPECTROSCOPIC AND MOLECULAR DOCKING STUDIES ON THE INTERACTION OF DIMETRIDAZOLE WITH HUMAN SERUM ALBUMIN

Journal of The Chilean Chemical Society

ZHANG, WANJU¹  XIONG, XUJIE¹  GE, YUSHU¹  LIU, YI²  WANG, FANG² 

[1] Huanggang Normal University, Huanggang, P. R. China;Wuhan University, Wuhan, P. R. China

关键词: dimetridazole;    human serum albumin;    fluorescence quenching;    molecular docking;    interaction.;   

DOI  :  10.4067/S0717-97072013000200016

学科分类：化学（综合）

来源: Sociedad Chilena de Quimica

【 摘 要 】

Dimetridazole (DMZ) is widely used for the therapeutic treatment of farmed animals and is suspected of being human carcinogens and mutagens. The interaction between DMZ and human serum albumin (HSA) was investigated systematically by fluorescence spectroscopy, synchronous fluorescence, three-dimensional fluorescence, CD spectroscopy, UV-vis absorption spectroscopy and molecular docking study. The results indicated that the probable quenching mechanism of HSA by DMZ was dynamic quenching. The corresponding thermodynamic parameters ΔH, ΔS and ΔG were calculated according to Van't Hoff equation. The results (ΔH = 65.10 kJ mol1 and ΔS = 295.65 J mol1 K1) indicated that the driving force between DMZ and HSA was mainly typical hydrophobic interaction. The conformation changes in the interaction were studied by synchronous fluorescence, CD spectroscopy and three-dimensional fluorescence spectra. The results revealed that the microenvironment and conformation of HSA has been changed. Molecular modeling study further confirmed the binding mode obtained by experimental study.

【 授权许可】

Unknown