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The interaction between thiazolo[2,3-b]pyrimidine (TZPM) analogues and bovine serum albumin (BSA) was investigated by fluorescence and UV–Vis spectroscopy.The experiment was explored at two different temperatures (299 and 307 K) under imitated physiological conditions.The results indicated that TZPM caused the fluorescence quenching of BSA through a combined quenching procedure.From the spectra obtained,the binding constant (Ka),binding sites (n) at different temperatures were calculated.Based on the F?rster non-radiation energy transfer theory,the average binding distance between BSA and TZPM was obtained.The synchronous fluorescence spectra indicated that the conformation of BSA has been changed.The comparison of binding potency of TZPM and BSA suggested that the substituent on the benzene ring enhance the binding affinity of TZPM and BSA.We investigated the possible sub-domain on BSA where bind TZPM by displacement experiments.Furthermore,to explore the effect of molecular structure on the binding,a study on quantitative structure-property relationship (QSPR) was performed.