光谱法研究单硝酸异山梨酯与牛血清白蛋白的相互作用

发布时间：2019-07-09 14:35

【摘要】：为研究单硝酸异山梨酯(IM)与牛血清白蛋白(BSA)之间的相互作用,用紫外-可见光谱法和荧光光谱法在优化的实验条件下进行研究。结果表明:IM与BSA形成基态复合物从而猝灭BSA的内源性荧光,猝灭机理为静态猝灭。通过计算得出IM与BSA的结合常数Kb及结合为点数n。根据热力学参数确定了IM和BSA之间的作用力类型主要为静电引力。生成自由能变驻G为负值,表明IM与BSA的作用过程是一个自发过程。同步荧光光谱表明IM对BSA构象产生很微弱的影响,使BSA腔内疏水环境的极性减弱。同步荧光光谱显示两者的结合位点更接近于酪氨酸,两者的结合部位主要位于亚螺旋域ⅢA中。Hill系数nH1,表明IM有正协同作用。为后续硝酸脂类药物的研发和进一步探讨IM在生物体内与蛋白质的作用机制和生物学效应提供了理论依据。
[Abstract]:In order to study the interaction between isosorbide mononitrate (IM) and bovine serum albumin (BSA), UV-Vis and fluorescence spectroscopy were used to study the results. The results show that IM and BSA form ground state complex to quench the endogenous fluorescence of BSA, and the quenching mechanism is static quenching. The binding constant Kb of IM and BSA and the combination of the number of points n are obtained. The force type between IM and BSA is determined to be the electrostatic attraction force according to the thermodynamic parameters. The generation of free energy variable in G is a negative value, indicating that the action process of IM and BSA is a spontaneous process. The synchronous fluorescence spectra show that IM has a very weak effect on the conformation of BSA, and the polarity of the hydrophobic environment in the BSA cavity is weakened. The simultaneous fluorescence spectrum shows that the binding sites of the two are closer to the tyrosine, and the binding sites of the two are mainly located in the sub-helical region IIIA. Hill factor, nH1, indicates that IM has a positive synergistic effect. This paper provides a theoretical basis for the development and further discussion of the mechanism and biological effects of IM in vivo and in vivo.
【作者单位】：曲靖师范学院化学化工学院;
【基金】：云南省教育厅科研项目(2012Y414) 国家自然科学基金资助项目(21261019)共同资助
【分类号】：R96

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