Spectroscopic and molecular docking studies on the interaction of dimetridazole with human serum albumin

• WANJU ZHANG ^[1] ; FANG WANG ^[1] ; XUJIE XIONG ^[1] ; YUSHU GE ^[2] ; YI LIU ^[2]
  1. [1] Huanggang Normal University

     Huanggang Normal University

     China

     
  2. [2] Wuhan University

     Wuhan University

     China

     
• Localización: Journal of the Chilean Chemical Society (Boletín de la Sociedad Chilena de Química), ISSN-e 0717-6309, ISSN 0366-1644, Vol. 58, Nº. 2, 2013, págs. 1717-1721
• Idioma: inglés
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• Resumen

  • 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.