This study investigates the interaction between tebuconazole and bovine serum albumin (BSA) in a physiological buffer (pH = 7.4) using the fluorescence quenching method to obtain the apparent binding constants (K) and number of binding sites (n) in the interaction between tebuconazole and BSA. The results revealed that tebuconazole can quench the intrinsic fluorescence of BSA through a static quenching procedure. It also shows that the thermodynamic parameters of enthalpy change (ΔH) and entropy change (ΔS) are negative, indicating that the interaction of tebuconazole with BSA is mainly driven by van der Waals forces and hydrogen bonds. The process of binding was a spontaneous process in which Gibbs free energy change was negative. The distance of r between the donor (BSA) and acceptor (tebuconazole) was calculated to be 0.68 nm based on Forster’s non-radiative energy transfer theory. Analysis of synchronous fluorescence, three-dimensional fluorescence and circular dichroism (CD) spectra demonstrates that tebuconazole can induce conformational changes of BSA.

本研究使用荧光猝灭法研究了戊酸叔丁唑与生理缓冲液（pH = 7.4）中的牛血清白蛋白（BSA）之间的相互作用，从而获得了戊酸叔丁康唑之间的表观结合常数（K）和结合位点数（n）和BSA。结果表明，戊唑醇可以通过静态猝灭程序猝灭BSA的固有荧光。还显示了焓变（ΔH）和熵变（ΔS）的热力学参数）为负值，表明戊唑醇与BSA的相互作用主要由范德华力和氢键驱动。结合过程是自发过程，吉布斯自由能变化为负。根据福斯特（Forster）的非辐射能量转移理论，供体（BSA）与受体（戊唑醇）之间的r距离为0.68 nm。同步荧光，三维荧光和圆二色性（CD）光谱分析表明，戊唑醇可以诱导BSA的构象变化。