Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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The Interaction of HIV-1 Inhibitor 3,3',3",3‴-Ethylenetetrakis-4-Hydroxycoumarin with Bovine Serum Albumin at Different pH

  • Dong, Sheying (College of Sciences, Xian University of Architecture and Technology) ;
  • Yu, Zhuqing (College of Sciences, Xian University of Architecture and Technology) ;
  • Li, Zhiqin (College of Sciences, Xian University of Architecture and Technology) ;
  • Huang, Tinglin (College of Environmental and Municipal Engineering, Xian University of Architecture and Technology)
  • Received : 2011.02.16
  • Accepted : 2011.05.03
  • Published : 2011.06.20
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Abstract

We studied the interaction of 3,3',3'',3'''-ethylenetetrakis-4-hydroxycoumarin (EHC) with bovine serum albumin (BSA) in acetate buffer and phosphate buffer with different pH values by UV-vis absorption spectrometry and fluorescence spectrometry respectively. It was found that the pH values of the buffer solutions had an effect on the interaction process. In acetate buffer of pH 4.70, the carbonyl groups in EHC bound to the amino groups in BSA by means of hydrogen bond and van der Waals force, which made the extent of peptide chain in BSA changed. By contrast, in phosphate buffer of pH 7.40, hydrophobic force played a major role in the interaction between EHC and BSA, while the hydrogen bond and van der Waals force were also involved in the interaction. The results of spectrometry indicated that BSA could enhance the fluorescence intensity of EHC by forming a 1:1 EHC-BSA fluorescent complex through static mechanism at pH 4.70 and 7.40 respectively. Furthermore, EHC bound on site 1 in BSA.

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