中文摘要：

应用光谱手段研究了在pH值7．4的生理酸度条件下氟氯氰菊酯（CF）与牛血清白蛋白（BSA）之间的相互作用。测定了不同温度下的猝灭常数，证实了在0．35μ4．16gmol／L的浓度范围内氟氯氰菊酯对BSA的内源荧光有较强的猝灭作用，机理为静态猝灭。计算了热力学参数，由焓变（△H）和熵变（△S）值推断氟氯氰菊酯与BSA之间主要靠疏水作用力结合，生成自由能变△G小于0，表明此作用过程是一个自发过程。结合过程中BSA构象的变化通过同步荧光和圆二色谱实验得以证实。圆二色谱实验的结果显示BSA中的α-螺旋结构损失了，说明其微环境及构象均发生了变化。

英文摘要：

The interaction of cyfluthrin （CF） and bovine serum albumin （BSA） under physiological condition was investigated by spectroscopic methods and the quenching constants at different temperatures were measured. The fluorescence results revealed that CF caused the fluorescence quenching of BSA through a static quenching procedure at low concentrations of CF ranging from 0.35-4.16 μmol/L. Thermodynamic parameters △G, △H and △S at different temperatures were calculated. The data indicated that the hydrophobic force was the dominant intermolecular force in stabilizing the complex and the binding process was spontaneous. In addition, the impact of CF on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy and circular dichroism spectroscopy. The CD spectra results showed that the α-helix content of BSA decreased. It was concluded that the microenvironment and conformation of BSA were changed in the binding reaction.