Study of the interaction between bovine serum albumin and analogs of Biphenyldicarboxylate by spectrofluorimetry.

This work was designed to study the interaction between bovine serum albumin (BSA) and Biphenyldicarboxylate (DDB) or analogs (I, II and III) of DDB by UV-visible and fluorescence spectroscopic methods for the first time. Results showed that both DDB and analogs had a strong ability to quench the intrinsic fluorescence of BSA through a static quenching procedure. The binding constants (K) were calculated according to the relevant fluorescence data. The thermodynamic parameters (ΔH, ΔS and ΔG) showed that the hydrophobic force played a major role in the binding interaction between BSA and DDB or analogs. Synchronous fluorescence spectra of BSA were investigated in the presence of DDB or analogs. It was showed that DDB was the strongest quencher and bound to BSA with the highest affinity among four compounds. The influence of molecular structure on the binding aspects was reported.