降龙涎二醇与牛血清白蛋白的相互作用研究

本论文以降龙涎二醇为研究对象,在模拟生理酸度的条件下,采用荧光猝灭法、紫外-可见吸收光谱法和红外光谱法,对降龙涎二醇与牛血清白蛋白(bovine serum albumin,BSA)的相互作用进行研究。降龙涎二醇对BSA荧光光谱的影响,结合常数与结合位点数,热力学的研究发现,降龙涎二醇对BSA内源荧光会进行猝灭,疏水作用力是该过程中的主要驱动力。降龙涎二醇在BSA上,与华法林共用一个结合位点。通过同步荧光光谱最大发射波长的监测,证实了降龙涎二醇可使酪氨酸环境的极性降低,疏水性增加,而色氨酸残基所处微环境的极性增加,疏水性降低。此外,综合紫外-可见吸收光谱、同步荧光光谱和红外光谱的分析结果,可以看出温度对降龙涎二醇与BSA的结合有影响,且降龙涎二醇的存在,能诱使BSA的微环境和构象发生改变,降低BSA的稳定性。

Study on the Interaction between Ambradiol and Bovine Serum Albumin

In this study, the interaction of ambradiol and bovine serum albumin (BSA) was investigated by fluorescence quenching, UV-Vis absorption spectroscopy and infrared spectroscopy under conditions of simulated physiological acidity. The effect of ambradiol on the fluorescence spectrum of BSA, the binding constant and the number of binding sites, thermodynamic studies presented that ambradiol quenched the endogenous fluorescence of BSA, and the hydrophobic interaction was the main driving force in the process. Ambradiol shared a binding site with warfarin on BSA. By monitoring the maximum emission wavelength of simultaneous fluorescence spectroscopy, it was confirmed that ambradiol can reduce the polarity of the tyrosine environment, increase the hydrophobicity, and increase the polarity of the microenvironment of the tryptophan residue and reduce the hydrophobicity. In addition, the results of UV-visible absorption spectroscopy, simultaneous fluorescence spectroscopy and infrared spectroscopy showed that temperature had an effect on the combination of norbornenediol and BSA, ambradiol could induced changes in microenvironment and conformation and reduced the stability of BSA.