College of Chemistry and Chemical Engineering, Mianyang Normal University, No. 30, Xianren Road, Youxian District, Mianyang, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2010 Oct 1;77(2):548-53. doi: 10.1016/j.saa.2010.06.016. Epub 2010 Jun 18.
In this paper, the interaction between flavonol p-coumaroylglucoside tiliroside and BSA was investigated by fluorescence quenching spectra, synchronous fluorescence spectra, and three-dimensional fluorescence spectra under simulative physiological conditions. It was proved that the fluorescence quenching of BSA by tiliroside was mainly a result of the formation of a tiliroside-BSA complex. The modified Stern-Volmer quenching constant and the corresponding thermodynamic parameters DeltaH, DeltaG and DeltaS at different temperatures were calculated. The results indicated that electrostatic interactions were the predominant intermolecular forces in stabilizing the complex. The distance r=3.95 nm between the donor (BSA) and acceptor (tiliroside) was obtained according to Förster's nonradioactive energy transfer theory. The synchronous fluorescence and three-dimensional fluorescence spectra results showed the microenvironment and conformation of BSA were changed in the binding reaction.
本文采用荧光猝灭光谱、同步荧光光谱和三维荧光光谱法，在模拟生理条件下研究了黄酮醇对香豆酰基葡萄糖基芹菜苷与牛血清白蛋白（BSA）的相互作用。结果表明，在模拟生理条件下，黄酮醇对香豆酰基葡萄糖基芹菜苷与 BSA 的荧光猝灭主要是由于形成了黄酮醇对香豆酰基葡萄糖基芹菜苷-BSA 复合物。计算了不同温度下的修正 Stern-Volmer 猝灭常数和相应的热力学参数ΔH、ΔG 和ΔS。结果表明，静电相互作用是稳定复合物的主要分子间作用力。根据福斯特非放射性能量转移理论，计算得到供体（BSA）和受体（黄酮醇对香豆酰基葡萄糖基芹菜苷）之间的距离 r=3.95nm。同步荧光和三维荧光光谱结果表明，在结合反应中 BSA 的微环境和构象发生了变化。
