Studying the interaction of bovine serum albumin with cefpirome sulfate by synchronous fluorescence spectroscopy

摘要

The interaction of cefpirome sulfate with bovine serum albumin in aqueous solution was studied by synchronous fluorescence and verified by fluorescence quenching spectroscopy. The data of synchronous fluorescence spectroscopy was used to infer the mechanism of the system and calculate the relevant parameters. The experimental results showed that the static mechanism played a role in the system; there was only one site for cefpirome sulfate on bovine serum albumin and me binding site was located in sub-domain IIA of BSA. Thermodynamic parameters were calculated, suggesting that hydrogen bond and hydrophobic interactions played a major role in stabilizing the complex. Based on the theory of Forester's non-radiation energy transfer, binding distance is < 7 nm. In addition, synchronous fluorescence spectroscopy also provided information about the change of the molecular environment.