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在pH为7.40的T ris-HC l缓冲体系中,采用荧光光谱技术研究了黄芩苷与牛血清白蛋白(BSA)的相互作用。随着温度升高,黄芩苷与牛血清白蛋白的猝灭常数逐渐增大,表明黄芩苷对BSA的荧光猝灭为动态猝灭过程,由结合过程的热力学参数ΔH=51.708 kJ.m o-l 1>0和ΔS=265.075J.m o-l 1.K-1>0,推断黄芩苷与BSA之间主要靠疏水作用力相结合,生成自由能变(ΔG)为负值,表明黄芩苷与BSA的作用过程是一个自发过程;应用同步荧光光谱考察了黄芩苷对BSA构象的影响。
Fluorescence spectroscopy was used to study the interaction of baicalin with bovine serum albumin (BSA) in a Tris-HCl buffer system at pH 7.40. With the increase of temperature, the quenching constant of baicalin and bovine serum albumin gradually increased, indicating that the fluorescence quenching of baicalin to BSA is a dynamic quenching process. The thermodynamic parameters ΔH = 51.708 kJ.mol 1 > 0 and ΔS = 265.075Jm ol 1.K-1> 0, it was concluded that the interaction between baicalin and BSA was mainly due to hydrophobic interaction, and the free energy change (ΔG) was negative, indicating the interaction between baicalin and BSA Is a spontaneous process. The effect of baicalin on the conformation of BSA was investigated by synchronous fluorescence spectroscopy.