烟酰胺与牛血清白蛋白相互作用的光谱研究。
Spectroscopic studies on the interaction between nicotinamide and bovine serum albumin.
作者信息
Xu Hui, Liu Quanwen, Wen Yanqing
机构信息
School of Chemistry and Materials Science, Ludong University, Yantai City, Shandong Province 264025, China.
出版信息
Spectrochim Acta A Mol Biomol Spectrosc. 2008 Dec 1;71(3):984-8. doi: 10.1016/j.saa.2008.02.021. Epub 2008 Feb 19.
The interaction of nicotinamide (NA) and bovine serum albumin (BSA) was studied by fluorescence and absorption spectroscopy at different temperatures. The results revealed that NA caused the fluorescence quenching of BSA through a static quenching procedure. The binding constants K(A), and the number of binding sites n, corresponding thermodynamic parameters DeltaG, DeltaH, DeltaS between NA and BSA at different temperatures were calculated. The primary binding pattern between NA and BSA was interpreted as hydrophobic interaction. In addition, the effect of NA on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. The binding average distance, r between the donor (BSA) and acceptor (NA) was determined based on the Förster's theory and it was found to be 3.1 nm.
在不同温度下，通过荧光光谱和吸收光谱研究了烟酰胺（NA）与牛血清白蛋白（BSA）的相互作用。结果表明，NA通过静态猝灭过程导致BSA的荧光猝灭。计算了不同温度下NA与BSA之间的结合常数K(A)、结合位点数n以及相应的热力学参数ΔG、ΔH、ΔS。NA与BSA之间的主要结合模式被解释为疏水相互作用。此外，使用同步荧光光谱分析了NA对BSA构象的影响。根据Förster理论确定了供体（BSA）与受体（NA）之间的结合平均距离r，发现其为3.1 nm。
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