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异甘草素是传统中药甘草中的重要活性成分之一,本工作的目的是明确异甘草素与牛血清蛋白之间的相互作用。我们讨论了异甘草素导致牛血清蛋白荧光淬灭的机制,通过荧光淬灭法测定了结合位点数n、表观结合常数K,计算了不同温度下的热力学常数ΔH~0,ΔG~0,ΔS~0。通过F?rster理论计算了异甘草素和牛血清蛋白之间的结合距离r,同步荧光光谱和紫外可见吸收光谱表明牛血清蛋白的结构发生了改变。
Isoliquiritigenin is one of the important active ingredients in traditional Chinese medicine licorice. The purpose of this work is to clarify the interaction between isoliquiritigenin and bovine serum albumin. We discussed the mechanism of isoliquiritigenin-induced fluorescence quenching of bovine serum albumin. The binding site number n and apparent binding constant K were determined by fluorescence quenching method. The thermodynamic constants ΔH ~ 0, ΔG ~ 0 at different temperatures were calculated, ΔS ~ 0. The binding distance between isoliquiritigenin and bovine serum albumin was calculated by F? Rster theory. Synchronous fluorescence and UV-Vis absorption spectra showed that the structure of bovine serum albumin changed.