酮康唑与血清白蛋白相互作用的荧光光谱研究

用荧光光谱和紫外吸收光谱法研究了酮康唑与牛血清白蛋白和人血清白蛋白的相互作用。实验进行于pH = 7.40±0.1的0.1 mol∙L-1PBS磷酸缓冲溶液。实验结果表明，酮康唑与牛血清白蛋白和人血清白蛋白的结合常数均会随着温度的升高而降低，酮康唑可以有规律地使血清白蛋白内源荧光猝灭，其猝灭机理可认为是酮康唑与白蛋白形成复合物的静态猝灭。并且获得了不同温度下，酮康唑与白蛋白作用的结合常数以及∆G、∆H和∆S等热力学参数。根据所得结果可推断酮康唑与白蛋白的作用力主要为静电作用力和疏水作用力，同时由FRET能量转移理论计算得出了酮康唑与白蛋白结合位置的距离r。

Study on the Interaction of Ketoconazole with Human and Bovine Serum Albumins by Fluorescence Spectroscopy

The binding of ketoconazole to human serum albumin and bovine serum albumin was studied by using fluorescence and ultraviolet spectroscopy. The measurements were performed in 0.1 mol·L^?1 phosphate buffer solution at pH=7.40±0.1. Decreasing of quenching constant was observed in association with temperature increase. Our findings show that the quenching mechanism of fluorescence of serum albumins by ketoconazole was static quenching because of compound formation. The thermodynamic parameters ΔG, ΔH, and ΔS at different temperatures were calculated, showing that the electrostatic interactions and hydrophobic interaction are the main forces for the binding of ketoconazole to serum albumins. The distance r between the donor (Trp‐214) and acceptor (ketoconazole) was obtained according to fluorescence resonance energy transfer theory.