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在模拟人体生理条件下,采用荧光光谱、紫外光谱、圆二色谱和分子模拟等多种技术和方法,研究了甘氨酸-水杨醛席夫碱和邻菲咯啉混合铜(Ⅱ)配合物(Cu GP)与牛血清白蛋白(BSA)相互作用的热力学行为.荧光光谱和紫外光谱分析表明,Cu GP与BSA之间的猝灭机制为复杂的混合猝灭机制.通过所获取的相互作用热力学参数,可以发现Cu GP与BSA的相互作用是一个吉布斯自由能降低的自发过程,猝灭过程的活化能为8.61 k J/mol,二者之间的主要作用力为静电相互作用力.圆二色谱的分析发现Cu GP与BSA的结合会导致蛋白结构发生破坏,其?-螺旋含量减少,无归卷曲含量升高.分子模拟研究发现Cu GP结合在BSA的Site?位点,与BSA发光残基TRP213,TYR156,TYR340和TYR451之间距离小于5?.
Under simulated human physiological conditions, the complexes of glycine-salicylaldehyde Schiff base with phenanthroline (Cu GP) were studied by fluorescence spectroscopy, UV spectroscopy, circular dichroism and molecular simulation. ) And bovine serum albumin (BSA) .Fluorescence spectroscopy and UV spectroscopy showed that the quenching mechanism between Cu GP and BSA is a complex mixed quenching mechanism.By the obtained thermodynamic parameters of interaction, It can be found that the interaction between Cu GP and BSA is a spontaneous process of Gibbs free energy decrease, the activation energy of quenching process is 8.61 kJ / mol, and the main interaction force between them is electrostatic interaction. Chromatography analysis showed that the binding of Cu-GP to BSA resulted in the destruction of the protein structure, the reduction of? -helix content and the increase of non-induced curl content. Molecular modeling showed that CuGP binds to BSA site at BSA, The distances between bases TRP213, TYR156, TYR340 and TYR451 are less than 5 ?.