Study on the interaction between propyl gallate and bovine serum albumin using fluorescence spectroscopy and molecular docking

The interaction between propyl gallate( PG) and BSA was studied by the spectroscopy method in vitro.The quenching mechanism was a static quenching procedure,and the binding constants KAbetween PG and BSA was obtained to be 1.03 × 105L·mol- 1while the binding distance was calculated as 2.2 nm at 299 K. The thermodynamic calculations suggested the van der Waals interactions and the hydrogen bonds play a major part in the interaction between BSA and PG.The further study of binding site showed there was one PG- binding site in the subdomain IIA of BSA. CD spectroscopic further showed that drug complexation altered protein conformation by a major reduction of α- helix inducing a partial protein destabilization. In addition,the result of autodocking for PG and BSA was simulated,and the parameters of the binding were accorded with the results of the calculation.