Study on the Binding Reaction Features Between Naphthol Green B and Bovine Serum Albumin by Fluorescence Spectrophotometry
YAN Cheng-nong1,XIE Ze-yu1,MEI Ping1,LIU Yi2
1. College of Chemistry and Enviornmental Engineering, Yangtze University, Jinzhou 434023, China 2. College of Chemistry and Molecule Sciences, Wuhan University, Wuhan 430072，China
Abstract：At different temperatures, the binding of naphthol green B(NGB) to bovine serum albumin (BSA) was studied by the fluorescence spectroscopy, three-dimensional fluorescence spectrum, synchronous fluorescence spectrum and ultra-violet spectrum. It was shown that this compound has a quite strong ability to quench the fluorescence from BSA. After analyzing the fluorescence quenching data according to Sterm-Volmer equation and Lineweaver-Burk equation, it was found that BSA had reacted with naphthol green B and formed a new compound, the quenching action was due to static fluorescence quenching, and the action force was electrostatic interaction. According to the Lineweaver-Burk equation and thermodynamic equation, the average value of the binding constant(KLB：1.411×105 L·mol-1)，the thermodynamic parameters(ΔHθ：-5.707 kJ·mol-1,ΔGθ：-30.25 kJ·mol-1 and ΔSθ：79.95 J·K-1) and the amounts of binding sites(1.258) were obtained, providing important information for the research on the configuration modification of BSA because of the added naphthol green B, biological effects in a living body, and the coloration mechanism of naphthol green B.
颜承农1,谢泽钰1,梅平1,刘义2 . 荧光光谱法研究萘酚绿B与牛血清白蛋白相互作用特征[J]. 光谱学与光谱分析, 2007, 27(12): 2542-2545.
YAN Cheng-nong1,XIE Ze-yu1,MEI Ping1,LIU Yi2 . Study on the Binding Reaction Features Between Naphthol Green B and Bovine Serum Albumin by Fluorescence Spectrophotometry . SPECTROSCOPY AND SPECTRAL ANALYSIS, 2007, 27(12): 2542-2545.
