论文部分内容阅读
用荧光光谱和紫外吸收光谱法,在pH=7.4±0.1的0.1mol·L-1磷酸缓冲溶液中,研究了伊曲康唑与牛血清白蛋白(BSA)和人血清白蛋白(HSA)的相互作用.实验结果表明,伊曲康唑与牛血清白蛋白和人血清白蛋白作用的猝灭常数均随着温度的升高而降低,伊曲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伊曲康唑与白蛋白形成复合物的静态猝灭.获得了在不同温度下,伊曲康唑与血清白蛋白作用的结合常数以及ΔG、ΔH和ΔS等热力学参数.根据所得结果可推断伊曲康唑与白蛋白的作用力主要为疏水作用力,同时,利用荧光共振能量转移理论(FRET)计算得出了伊曲康唑与白蛋白结合位置的距离d.而且,利用同步荧光光谱和紫外光谱揭示了该反应中蛋白的结构和其微环境的变化.
Fluorescence spectroscopy and ultraviolet absorption spectroscopy were used to study the effects of itraconazole and bovine serum albumin (BSA) and human serum albumin (HSA) in 0.1 mol·L-1 phosphate buffer solution at pH = 7.4 ± 0.1 The experimental results show that the quenching constant of itraconazole and bovine serum albumin and human serum albumin all decrease with the increase of temperature, itraconazole can regularly make the serum albumin endogenous Fluorescence quenching, the quenching mechanism can be considered as the static quenching of itraconazole and albumin complex obtained.Under different temperatures, the binding constants of itraconazole and serum albumin and ΔG, ΔH and ΔS and other thermodynamic parameters.According to the results obtained, we concluded that the interaction between itraconazole and albumin is mainly hydrophobic and that the position of itraconazole binding to albumin is calculated by the fluorescence resonance energy transfer theory (FRET) Furthermore, the changes of the structure and microenvironment of the protein in the reaction were revealed by synchronous fluorescence spectroscopy and UV spectroscopy.