Study on the interaction between thiazolopyrimidine analogues and bovine serum albumin

Fluorescence and ultraviolet spectroscopy were used to explore the interaction between thiazolopyrimidines (TAPM) and bovine serum albumin (BSA) under imitated physiological conditions. The experimental results show that thiazolopyrimidines can quench the fluorescence of BSA through a static quenching process. The binding constants, binding sites, and thermodynamic parameters at different temperatures were calculated. The calculated results indicate that the interaction between thiazolopyrimidines and BSA is driven mainly by Van der Waals' force and hydrogen bonds. The binding distances r was obtained based on F?rster theory of non-radiation energy transfer. The comparison of binding potency of thiazolopyrimidines and BSA suggests that the substituent on the benzene ring promotes the binding process of thiazolopyrimidines and BSA.