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目的研究毛蕊花糖苷(verbascoside,VER)与牛血清白蛋白(bovine serum albumin,BSA)的分子作用机制。方法生理条件下,光谱法测定VER与BSA的相互作用参数,分子模拟建立VER-BSA结合模型,分析其结合反应机制。结果构建的VER-BSA模型表明,维持VER与BSA的相互作用力主要是氢键和范德华力,兼有疏水作用力。光谱实验表明VER与BSA的相互作用为静态结合过程,结合强度较强,VER与BSA的结合距离(r)值较小,说明发生了能量转移现象。VER对BSA的结构域微区构象产生影响,使结合位域的疏水性发生改变。解析荧光相图得出VER与BSA反应构象型态的变迁为“二态”模型。热力学参数表明VER与BSA的相互作用是以氢键和范德华力为主的分子间作用。荧光偏振定量证明BSA与VER相互作用中生成了非共价复合物。结论光谱实验与计算机模拟结果一致,可为研究VER与BSA分子作用机制提供一定参考。
Objective To study the molecular mechanism of verbascoside (VER) and bovine serum albumin (BSA). Methods Under physiological conditions, the interaction parameters between VER and BSA were determined by spectrometry. The VER-BSA binding model was established by molecular simulation and the binding reaction mechanism was analyzed. Results The VER-BSA model established showed that the interaction between VER and BSA was mainly hydrogen bonding and van der Waals forces, both of which were hydrophobic. Spectral experiments show that the interaction between VER and BSA is a static binding process, the binding strength is strong, and the binding distance (r) between VER and BSA is small, indicating that energy transfer occurs. VER affects the domain domain conformation of BSA and changes the hydrophobicity of the binding domain. The fluorescence phase diagram was analyzed to show that the change in the conformational pattern of the reaction between VER and BSA was a “binary state” model. The thermodynamic parameters indicate that the interaction between VER and BSA is an intermolecular interaction dominated by hydrogen bonding and van der Waals forces. Fluorescence polarization quantification demonstrates that non-covalent complexes are formed in the BSA-VER interaction. Conclusions The results of spectral experiments are in good agreement with those of computer simulations, which may provide some references for studying the mechanism of action of VER and BSA.