The interaction between BSA and compound 1 was studied by UV–vis, fluorescence and circular dichroism spectroscopy under physiological conditions (pH = 7.4). Molecular docking and molecular dynamics analyses were also performed. The results showed that compound 1 could bind to BSA. When compound 1 bound to BSA, there were a series of changes in the spectral properties of BSA, which were an enhancement effect of the UV–Vis spectrum of BSA, fluorescence quenching and a weak conformational change in the CD spectrum. The results of the fluorescence experiments at 298, 303 and 310 K showed that fluorescence quenching caused by the addition of compound 1 to BSA was generally static quenching accompanied by a dynamic quenching process, which was shown by the quenching constants of 2.010 × 10⁴ L∙M⁻¹, 1.850 × 10⁴ L∙M⁻¹, and 1.970 × 10⁴ L∙M⁻¹ at the three different temperatures, respectively. From the obtained binding constants and thermodynamic parameters, it was found that hydrophobic forces played an important role in the binding process of 1 to BSA. The results of synchronous fluorescence and three-dimensional fluorescence showed that compound 1 caused a weak conformational change in BSA. Docking results showed that compound 1 was located at binding site II of bovine serum albumin protease. In addition, the flavonoid moiety of compound 1 contributes to the hydrophobic binding of compound 1 to BSA. The results of molecular dynamics, including the root-mean-square deviation (RMSD) and RMS fluctuation (RMSF) values, showed that the binding of compound 1 to BSA did not cause a significant conformational change in BSA.

在生理条件下（pH = 7.4），通过紫外可见光谱，荧光和圆二色光谱研究了牛血清白蛋白与化合物1之间的相互作用。还进行了分子对接和分子动力学分析。结果表明化合物1可以结合BSA。当化合物1与BSA结合时，BSA的光谱特性发生了一系列变化，包括BSA的UV-Vis光谱增强，荧光猝灭和CD光谱中的弱构象变化。298、303和310 K的荧光实验结果表明，加入化合物1导致荧光猝灭到BSA普遍静态猝灭伴随有动态淬火处理，将其通过的2.010×10的猝灭常数所示⁴ 大号∙中号^-1，1.850×10 ⁴ 大号∙中号^-1，和1.970×10 ⁴ 大号∙中号^{- 1}在三个不同的温度下，分别。从获得的结合常数和热力学参数，发现疏水力在1-与BSA的结合过程中起重要作用。同步荧光和三维荧光的结果表明，化合物1在BSA中引起了较弱的构象变化。对接结果表明，化合物1位于牛血清白蛋白蛋白酶的结合位点II。另外，化合物1的类黄酮部分有助于化合物1与BSA的疏水结合。分子动力学的结果，包括均方根偏差（RMSD）和RMS波动（RMSF）值，表明化合物1与BSA的结合不会引起BSA的显着构象变化。