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通过紫外光谱法、荧光光谱法和圆二色谱法研究了异黄酮类小分子(大豆素和葛根素)与人血清白蛋白的结合常数、结合位点及结合距离等相互作用机制。结果发现在具有相同结合位点的情况下葛根素与人血清白蛋白的结合能力高于大豆素,主要归因于在相同的母核结构上葛根素比大豆素多一个葡萄吡喃糖基,导致反应的结合能力不同。且经过计算得知,异黄酮分子通过形成不发光复合物和F 0··rster能量转移使人血清白蛋白发生静态猝灭。圆二色光谱中葛根素使蛋白质中的α-螺旋含量增加,蛋白结构更加紧密导致蛋白质构象发生变化。研究结果表明:葛根素与人血清白蛋白的特异性结合能力高于大豆素,这对于临床医学、制药学等都具有十分重要的意义。
The interaction mechanism of binding constant, binding site and binding distance of isoflavone small molecules (daidzin and puerarin) with human serum albumin was studied by ultraviolet spectroscopy, fluorescence spectroscopy and circular dichroism spectroscopy. As a result, it was found that the binding ability of puerarin to human serum albumin is higher than that of daidzein with the same binding site, mainly due to the addition of one glucopyranosyl group of puerarin on the same mother nucleus structure, Lead to different reaction binding capacity. It has also been calculated that isoflavone molecules undergo static quenching of human serum albumin by the formation of a non-luminescent complex and F 0 ··· rster energy transfer. Circular dichroism in the puerarin protein in the α-helix content increases, the protein structure more closely lead to changes in protein conformation. The results show that: puerarin and human serum albumin binding specificity higher than that of daidzein, which for clinical medicine, pharmaceutical and so has a very important significance.