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Citation: CHI Yan-Hua, ZHUANG Jia, BI Xin-Ying, ZHOU Lei. Interaction of Diethylmalonylurea and Bovine Serum Albumin Studied by Fluorescence Method[J]. Chinese Journal of Applied Chemistry, ;2007, 24(10): 1167-1171. shu

Interaction of Diethylmalonylurea and Bovine Serum Albumin Studied by Fluorescence Method

1.
a Department of Chemistry, Southwest University of Science and Technology, MianYang 621010;
2.
b Department of Materials Science and Engineering, Southwest Petroleum University, Chengdu

Corresponding author: CHI Yan-Hua,
Received Date: 19 November 2006
Available Online: 20 March 2007
Fund Project: 国家电分析化学重点实验室基金项目(2005007) (2005007)四川省科学技术重点攻关项目(03GG009-024) (03GG009-024)

The interaction mechanism of diethylmalonylurea(BBT) with bovine serum albumin(BSA) was studied by fluorescence and UV-Vis spectra. It is shown that BBT has a powerful ability to quench the fluorescence intensity of BSA. The fluorescence quenching data were analyzed according to Stern-Volmer equation and Line weaver-Burk equation at 17℃ and 37℃ to obtain the quenching constants, ^17℃K_SV=1.427×10⁴ and ^37℃K_SV=1.195×10⁴, ^17℃K_LB=9.848×10³ and ^37℃K_LB=1.778×10³, and the binding constant K₀=4.341×10⁴, and the thermodynamic parameters(ΔH, ΔS and ΔG). It was deduced that combining site n was 1.136. The increasing of temperature was favorable for the BBT-BSA interaction. According to the thermodynamic parameters, the major binding forces were determined. The effect of BBT on the conformation of BSA was analyzed Via synchronous fluorescence spectroscopy.
- diethylmalonylurea(BBT),
- bovine serum albumin(BSA),
- fluorescence spectrometry,
- thermodynamic parameter
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