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首页> 外文期刊>Journal of Biomolecular Structure and Dynamics >In vitro study on binding interaction of quinapril with bovine serum albumin (BSA) using multi-spectroscopic and molecular docking methods
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In vitro study on binding interaction of quinapril with bovine serum albumin (BSA) using multi-spectroscopic and molecular docking methods

机译：用多光谱和分子对接方法在体外研究Quinapril与牛血清白蛋白（BSA）的结合相互作用

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摘要

The binding interaction between quinapril (QNPL) and bovine serum albumin (BSA) in vitro has been investigated using UV absorption spectroscopy, steady-state fluorescence spectroscopic, synchronous fluorescence spectroscopy, 3D fluorescence spectroscopy, Fourier transform infrared spectroscopy, circular dichroism, and molecular docking methods for obtaining the binding information of QNPL with BSA. The experimental results confirm that the quenching mechanism of the intrinsic fluorescence of BSA induced by QNPL is static quenching based on the decrease in the quenching constants of BSA in the presence of QNPL with the increase in temperature and the quenching rates of BSA larger than 10(10)Lmol(-1)s(-1), indicating forming QNPL-BSA complex through the intermolecular binding interaction. The binding constant for the QNPL-BSA complex is in the order of 10(5)M(-1), indicating there is stronger binding interaction of QNPL with BSA. The analysis of thermodynamic parameters together with molecular docking study reveal that the main binding forces in the binding process of QNPL with BSA are van der Waal's forces and hydrogen bonding interaction. And, the binding interaction of BSA with QNPL is an enthalpy-driven process. Based on Forster resonance energy transfer, the binding distance between QNPL and BSA is calculated to be 2.76nm. The results of the competitive binding experiments and molecular docking confirm that QNPL binds to sub-domain IIA (site I) of BSA. It is confirmed there is a slight change in the conformation of BSA after binding QNPL, but BSA still retains its secondary structure -helicity.
机译：使用UV吸收光谱，稳态荧光光谱，同步荧光光谱，3D荧光光谱，傅里叶变换红外光谱，圆形二色性和分子对接，研究了QuinaPRil（QNPL）和牛血清白蛋白（BSA）之间的结合相互作用。用BSA获得QNPL绑定信息的方法。实验结果证实，QNPL诱导的BSA的内在荧光的猝灭机制是基于BNPL在QNPL的存在下的淬火常数随温度的增加和大于10的淬火速率的降低（ 10）LMOL（-1）S（-1），表明通过分子结合相互作用形成QNPL-BSA复合物。 QNPL-BSA复合物的结合常数为10（5）m（-1）的量级，表明QnPL与BSA具有更强的结合相互作用。热力学参数与分子对接研究的分析表明，具有BSA的QNPL结合过程中的主要结合力是范德华的力和氢键相互作用。并且，BSA与QNPL的结合相互作用是焓驱动的过程。基于Forster Arsonance能量转移，QNPL和BSA之间的结合距离计算为2.76nm。竞争性结合实验和分子对接的结果证实QNPL与BSA的亚域IIA（位点I）结合。确认在结合QNPL后，BSA的构象存在略有变化，但是BSA仍然保持其二级结构 - 柔性。

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