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首页> 外文期刊>RSC Advances >Interaction between carisoprodol and bovine serum albumin and effect of beta-cyclodextrin on binding: insights from molecular docking and spectroscopic techniques
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Interaction between carisoprodol and bovine serum albumin and effect of beta-cyclodextrin on binding: insights from molecular docking and spectroscopic techniques

机译：Carisoprodol与牛血清白蛋白之间的相互作用以及β-环糊精对结合的影响：分子对接和光谱技术的见解

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摘要

Biomolecular interactions of carisoprodol (CAP) with bovine serum albumin (BSA) have been studied by fluorescence and UV-visible spectroscopy and confirmed by multispectroscopic methods including molecular docking studies. The intrinsic intensity of BSA was quenched by a dynamic quenching mechanism. The binding constant and number of binding sites were calculated according to the Stern-Volmer equation. The effect of beta-cyclodextrin on the binding has been studied. Thermodynamic parameters were calculated which reveal the involvement of hydrophobic interactions in the binding. Based on Forster's theory of non-radiation energy transfer, the average binding distance (r) between BSA and CAP was evaluated. Spectral results showed that the binding of CAP to BSA induced conformational changes in BSA. A molecular docking study confirmed the drug binding sites and interaction of CAP with amino acid residues.
机译：Carisoprodol（CAP）与牛血清白蛋白（BSA）的生物分子相互作用已通过荧光和紫外可见光谱法进行了研究，并通过包括分子对接研究在内的多光谱方法得到了证实。 BSA的固有强度通过动态淬灭机制淬灭。根据Stern-Volmer方程计算结合常数和结合位点数。已经研究了β-环糊精对结合的影响。计算了热力学参数，其揭示了结合中疏水相互作用的参与。基于Forster的非辐射能量转移理论，评估了BSA和CAP之间的平均结合距离（r）。光谱结果表明，CAP与BSA的结合诱导了BSA的构象变化。一项分子对接研究证实了药物的结合位点以及CAP与氨基酸残基的相互作用。

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