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中文摘要：
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1.260×106 L·mol-1（292 K）和3.881×104 L·mol-1（311 K），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。
英文摘要：
Objective：To study the interaction of bovine serum albumin（BSA） with anticancer drug hydroxycamptothecin（HCPT） by fluorescence quenching spectra and synchronous fluorescence spectra.Methods：The Stern-Volmer curve and double logarithm equation and F？rster theory of non-radiation energy transfer was used to deal with the dates of fluorescence quench,and the synchronous spectrum was used to investigate the conformational changes of BSA.Results： The binding distances（r） of hydroxycamptothecin to BSA was 3.08 nm（292 K）;the binding constants（Kb） were 1.260×106 L·mol-1（292 K） and 3.881×104 L·mol-1（311 K）,respectively.The thermodynamic parameters △rHm〉0,△rSm〉0 and △rGm〈0. Conclusion：The static quenching exits between BSA and anticancer drug hydroxycamptothecin super-molecular complex,and interaction of them is mainly driven by hydrophobic force.
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