Aim: To study the interaction mechanism of bovine serum albumin (BSA) with luteolin and apigenin.
Methods: Fluorescence quenching method and non-radioactive energy transfer theory were used.
Results: The binding constants at different temperature were determined and the quenching mechanism of them were suggested as static quenching. The transfer efficiency of energy and distance between BSA and luteolin or apigenin were investigated according to the mechanism of the Förster energy transference.
Conclusion: The interaction between them seems to be strong and the binding force were mainly hydrophobic force. B(3')-OH,B(4')-OH strengthened the interaction of flavonoids and BSA.