The interaction of Solifenacin succinate (SFS) with bovine serum albumin (BSA) has been investigated by UV-visible spectrophotometric, spectrofluorometric viscometric and molecular modeling methods. Fluorescence spectra suggested that the quenching mechanism of the interaction of SFS to BSA was a static quenching type. By the analysis of UV/vis spectra, it was observed that SFS had a high affinity with BSA which was indicated by the large binding constant. The thermodynamic parameters, ΔH and ΔS for the interaction of SFS and BSA have been calculated at different temperatures. The thermodynamic studies suggested that the interaction processes were endothermic disfavoured (ΔH > 0) and entropy favoured (ΔS > 0), which indicated that the SFS might interact with BSA by a non-traditional intercalation mode of binding via hydrophobic force. Moreover, the results obtained from molecular docking corroborate the experimental results obtained from spectroscopic investigations.

中文翻译：

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用光谱技术和分子模型研究琥珀酸索利那新与牛血清白蛋白的相互作用

琥珀酸索利那新 (SFS) 与牛血清白蛋白 (BSA) 的相互作用已通过紫外-可见分光光度法、荧光分光光度计粘度计和分子建模方法进行了研究。荧光光谱表明SFS与BSA相互作用的猝灭机制是静态猝灭类型。通过紫外/可见光谱分析，观察到 SFS 与 BSA 具有高亲和力，这由大的结合常数表明。在不同温度下计算了 SFS 和 BSA 相互作用的热力学参数ΔH和ΔS。热力学研究表明，相互作用过程是不利于吸热的（Δ H > 0）和有利于熵的（Δ S> 0)，这表明 SFS 可能通过疏水力结合的非传统嵌入模式与 BSA 相互作用。此外，从分子对接获得的结果证实了从光谱研究中获得的实验结果。