Competitive binding of small molecules with biopolymers: a fluorescence spectroscopy and chemometrics study of the interaction of aspirin and ibuprofen with BSA

Abstract

The interaction of aspirin and ibuprofen with bovine serum albumin (BSA) was studied by spectrofluorimetry under simulated physiological conditions. Both aspirin and ibuprofen quenched the intrinsic fluorescence of BSA and the binding ratios obtained were 2 : 1 for aspirin–BSA and 3 : 1 for ibuprofen–BSA interactions, respectively. The thermodynamic parameters (ΔH, ΔS and ΔG) obtained from the fluorescence spectroscopy data showed that the binding of aspirin to BSA involved van der Waals interactions and hydrogen bonds. Competitive experiments using warfarin and diazepam as site markers indicated that aspirin was mainly located in the hydrophobic pocket of site II of the protein as well as to a small extent in site I. Furthermore, the competitive interaction of the aspirin and ibuprofen with BSA, which was studied with the use of the three-way excitation–emission fluorescence spectra and a parallel factor analysis (PARAFAC) chemometrics method, showed that the competitive effect of ibuprofen was stronger than that of aspirin, i.e. the former molecule replaced the aspirin from the aspirin–BSA complex.