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用光谱手段研究了在pH=7.4的生理酸度条件下农药氟氰戊菊酯(FC)与牛血清白蛋白(bovine serumalbumin,BSA)之间的相互作用.荧光研究表明,FC浓度的增加会引起BSA342 nm处荧光有规律地猝灭.采用Stern-Vol mer方程分析了猝灭的机理为静态猝灭.计算了热力学参数,由焓变(ΔH<0)和熵变(ΔS<0)值推断FC与BSA之间主要靠氢键和范德华力结合.生成自由能变ΔG<0,表明此作用过程是一个自发过程.通过同步荧光和圆二色谱实验证实了结合过程中BSA构象的变化.圆二色谱实验的结果显示了BSA中的α-螺旋结构的损失,说明其微环境及构象均发生了变化.
The interaction between flucythrinate (FC) and bovine serumalbumin (BSA) was studied spectroscopically at physiological pH of 7.4. Fluorescence studies showed that the increase of FC concentration caused The quenching mechanism was quenched by Stern-Volmer equation, and the thermodynamic parameters were calculated and deduced from enthalpy change (ΔH <0) and entropy change (ΔS <0) The bond between BSA and BSA mainly depends on hydrogen bonds and van der Waals forces, and the formation of free energy changes ΔG <0, indicating that this process is a spontaneous process.The conformation of BSA during the binding process was confirmed by synchronous fluorescence and circular dichroism The results of the two chromatographic experiments show the loss of α-helical structure in BSA, which shows that the microenvironment and conformation have changed.