Abstract: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.
