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目的:采用荧光光谱技术研究羟基喜树碱与牛血清白蛋白(BSA)的相互作用。方法:根据292 K和311 K时羟基喜树碱对BSA的荧光猝灭作用,利用Stern-Volmer方程,双倒数方程以及F rster非辐射能量转移理论处理实验数据,采用同步荧光光谱探讨了羟基喜树碱对BSA构象的影响。结果:羟基喜树碱与BSA间的结合距离r=3.08 nm(292 K),结合常数(Kb)为1.260×106L.mol-1(292K)和3.881×104L.mol-1(311K),羟基喜树碱与BSA结合的热力学参数△rHm>0,△rSm>0,△rGm<0。结论:羟基喜树碱对BSA的荧光猝灭作用属于静态猝灭,二者主要靠疏水作用力结合。
Objective: To study the interaction between hydroxycamptothecin and bovine serum albumin (BSA) by fluorescence spectroscopy. Methods: According to the fluorescence quenching of BSA by hydroxycamptothecin at 292 K and 311 K, the experimental data were treated by Stern-Volmer equation, double reciprocal equation and F rster non-radiative energy transfer theory. Effect of the alkali on BSA conformation. Results: The binding distances between hydroxycamptothecin and BSA were 3.08 nm (292 K) and 1.260 × 106 L · mol-1 (292 K) and 3.881 × 104 L · mol-1 (311 K) The thermodynamic parameters △ rHm> 0, △ rSm> 0 and △ rGm <0 for the binding of camptothecin and BSA. CONCLUSION: The fluorescence quenching of BSA by hydroxycamptothecin belongs to static quenching, and the two mainly depend on hydrophobic interaction.