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在模拟生理条件下应用荧光光谱学方法分别研究了淫羊藿苷和淫羊藿次苷Ⅰ与牛血清白蛋白(BSA)间的结合作用.根据荧光强度数据,计算出了结合常数KA,结合位点数n和热力学参数(△G,△H和△S).实验结果表明,淫羊藿苷和淫羊藿次苷Ⅰ都能显著猝灭BSA的内源荧光,猝灭机制均为形成基态复合物的单一静态猝灭过程.不同温度下(17℃,27℃,37℃)得到的KA和n值,表明淫羊藿次苷Ⅰ与BSA的结合强于淫羊藿苷.从得到的热力学参数判断,淫羊藿苷与BSA间的主要作用力是氢键作用和范德华力,而疏水作用和静电引力在淫羊藿次苷Ⅰ与BSA形成复合物过程中起主导作用.而且同步荧光光谱显示,淫羊藿苷和淫羊藿次苷Ⅰ与BSA的结合导致BSA构象发生了变化.
Fluorescence spectroscopy was used to study the binding of icariin and icariside Ⅰ to bovine serum albumin (BSA) under simulated physiological conditions.According to the fluorescence intensity data, the binding constant KA Site number n and thermodynamic parameters (△ G, △ H and △ S) .Experimental results show that icariin and icaritin Ⅰ can significantly quench the endogenous fluorescence of BSA, the quenching mechanism is the formation of ground state The single static quenching process of the complex.KA and n values obtained at different temperatures (17 ° C, 27 ° C, 37 ° C) indicate that the binding of Icariin I to BSA is stronger than that of Icariin According to the thermodynamic parameters, the main interaction between icariin and BSA was hydrogen bonding and van der Waals forces, while the hydrophobic and electrostatic attraction played a leading role in the formation of complexes of icariin Ⅰ with BSA. And synchronous fluorescence Spectra show that the binding of icariin and iridoside I to BSA results in a change in BSA conformation.