【摘要】 应用紫外光谱法和荧光光谱法研究了乙二胺四乙酸铁(Ⅲ)(EDTA-Fe(Ⅲ))与牛血清白蛋白的相互作用.结果表明:EDTA-Fe(Ⅲ)可以进入牛血清白蛋白的疏水腔,使蛋白质非极性区的生色基暴露于极性溶剂;EDTA-Fe(Ⅲ)通过静态猝灭的方式使牛血清白蛋白的荧光强度显著降低;EDTA-Fe(Ⅲ)与牛血清白蛋白主要以氢键和范德华力相结合.测定了EDTA-Fe(Ⅲ)与牛血清白蛋白的结合常数KA和结合位点数n,利用Forster非辐射能量转移机制确定了牛血清白蛋白与EDTA-Fe(Ⅲ)的结合距离和能量转移效率,并使用同步荧光技术探讨了EDTA-Fe(Ⅲ)对牛血清白蛋白构象的影响.更多还原

【Abstract】 The mechanism of action between EDTA-Fe(Ⅲ) and bovine serum albumin(BSA) was studied by ultraviolet spectra and fluorescence spectra.The results indicated that EDTA-Fe(Ⅲ) could invade the hydrophobic pocket of BSA,which made nonpolar chromophore of BSA be exposed to polar solvent.It was shown that the fluorescence intensity of BSA could be apparently quenched by EDTA-Fe(Ⅲ) based on static quenching model.The binding of EDTA-Fe( Ⅲ) and BSA was principally performed by means of the hydrophobic force and Van der Waals force.The binding constant KAvalues and the binding site n values were determined.The binding distance and the energy transfer efficiency between EDTA-Fe(Ⅲ) and BSA were obtained based on the theory of Forster’s non-radiative energy transfer.The effect of EDTA-Fe( Ⅲ) on the conformation ofBSA was further analyzed by using synchronous fluorescence spectrometry.更多还原