College of Environmental Science, Liaoning University, Shenyang, People's Republic of China.
Institute of Applied Ecology, Chinese Academy of Sciences, Shenyang, People's Republic of China.
J Environ Sci Health B. 2020;55(6):509-516. doi: 10.1080/03601234.2020.1725358. Epub 2020 Feb 10.
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 () and number of binding sites () 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 (Δ) and entropy change (Δ) 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 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.
本研究采用荧光猝灭法研究了唑菌酯与牛血清白蛋白（BSA）在生理缓冲液（pH = 7.4）中的相互作用，以获得唑菌酯与 BSA 相互作用的表观结合常数（）和结合位点数（）。结果表明，唑菌酯可以通过静态猝灭过程猝灭 BSA 的内源性荧光。还表明，焓变（Δ）和熵变（Δ）的热力学参数为负，表明唑菌酯与 BSA 的相互作用主要是由范德华力和氢键驱动的。结合过程是一个自发过程，吉布斯自由能变化为负。根据福斯特非辐射能量转移理论，计算出供体（BSA）和受体（唑菌酯）之间的距离（）为 0.68nm。同步荧光、三维荧光和圆二色性（CD）光谱分析表明，唑菌酯可以诱导 BSA 的构象变化。
