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为了解决盐酸文拉法辛荧光光谱与牛血清白蛋白(BSA)荧光光谱严重重叠的缺陷,在模拟人体生理条件下(p H 7.4 Tris-HCl缓冲液),以盐酸文拉法辛为荧光检测对象,BSA为猝灭剂,通过荧光光谱法研究了它们之间的相互作用。盐酸文拉法辛与BSA通过疏水作用力形成了一种稳定的复合物;由探针实验确定盐酸文拉法辛在BSA上的结合位点为位点Ⅰ;298K时结合常数为3.76×105L/mol,结合位点数约为1;Hill系数表明盐酸文拉法辛的药效受到温度的调控。利用分子对接技术模拟研究了二者的相互作用,其结果与光谱法获得的结果一致。
In order to solve the defect that the fluorescence spectrum of venlafaxine hydrochloride overlaps with the fluorescence spectrum of bovine serum albumin (BSA), the fluorescence of venlafaxine hydrochloride was detected under simulated human physiological conditions (p H 7.4 Tris-HCl buffer) Object, BSA as a quencher, the interaction between them was studied by fluorescence spectroscopy. Venlafaxine hydrochloride and BSA formed a stable complex by hydrophobic interaction; the binding site of venlafaxine hydrochloride on BSA was determined by probe experiments to be site I; the binding constant at 298K was 3.76 × 10 5 L / mol, the number of binding sites is about 1. The Hill coefficient indicates that the efficacy of venlafaxine hydrochloride is regulated by temperature. The molecular docking technique was used to simulate the interaction between the two. The results are consistent with those obtained by spectroscopy.