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首页> 外文期刊>Journal of Photochemistry and Photobiology, B. Biology: Official Journal of the European Society for Photobiology >Investigation of the interaction of a polyamine-modified flavonoid with bovine serum albumin (BSA) by spectroscopic methods and molecular simulation
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Investigation of the interaction of a polyamine-modified flavonoid with bovine serum albumin (BSA) by spectroscopic methods and molecular simulation

机译：通过光谱法和分子模拟对牛血清白蛋白（BSA）与牛血清白蛋白（BSA）相互作用的研究

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摘要

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 x 10(4) L.M-1, 1.850 x 10(4) L.M-1, and 1.970 x 10(4) 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.
机译：在生理条件下通过UV-Vis，荧光和圆形二色性光谱研究BSA和化合物1之间的相互作用（pH = 7.4）。还进行了分子对接和分子动力学分析。结果表明，化合物1可以与BSA结合。当化合物1与BSA结合时，BSA的光谱性能存在一系列变化，这是BSA的UV-Vis光谱的增强效果，CD光谱中的CD光谱的弱构象变化。在298,303和310k处的荧光实验结果表明，通过加入化合物1至BSA引起的荧光猝灭通常是静态猝灭，伴随动态猝灭过程，其由2.010×10的淬火常数显示（4 ）LM-1,1.850×10（4）LM-1和3.970×10（4）LM-1分别在三种不同的温度下。从获得的结合常数和热力学参数来看，发现疏水力在1至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引起弱构象变化。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至BSA的疏水结合。分子动力学的结果，包括根平均方偏差（RMSD）和RMS波动（RMSF）值，表明化合物1至BSA的结合在BSA中没有引起显着的构象变化。

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