咪唑斯汀与牛血清白蛋白的作用研究

目的研究咪唑斯汀与牛血清白蛋白(BSA)的相互作用机制和作用类型。方法用荧光光谱法检测Stern-Volmer猝灭常数,用紫外分光光度法(UV)和圆二色谱法(CD)检测咪唑斯汀对牛血清白蛋白构象的影响。结果用上述检测方法获得不同温度下咪唑斯汀与牛血清白蛋白的猝灭常数和热动力学参数。结论静态猝灭是咪唑斯汀导致BSA荧光猝灭的主要原因。不同温度下计算的热动力学参数表明,咪唑斯汀与牛血清白蛋白分子间的结合力以疏水作用力为主。上述二者的结合导致BSA的构象发生改变。

Study on the Interaction of Mizolastine with Bovine Serum Albumin

Objective The interaction of mizolastine with bovine serum albumin(BSA) was investigated with quenching of BSA fluorescence by mizolastine.Methods Fluorescence spectroscopy was employed to study the Stern-Volmer quenching constants(Ksv) of BSA in the presence of mizolastine in pH 7.4 PBS.The CD and UV absorption spectra were used to investigate the effect of mizolastine on the conformation of BSA.Results The quenching constants(Ksv) and corresponding thermodynamic parameters(ΔH,ΔS and ΔG) were calculated from the spectroscopic data at different temperatures.Conclusion The Ksv suggests that the quenching of BSA fluorescence by mizolastine occurs through the static process.The ΔH,ΔS and ΔG obtained at different temperatures show that the binding of mizolastine to BSA is mainly driven by hydrophobic force.The addition of mizolastine leads to the conformational changes of BSA.