Comparative Studies on the Interaction of Aspirin with Bovine Serum Albumin by Fluorescence Quenching Spectroscopy and Synchronous Fluorescence Spectroscopy

The interaction of aspirin with bovine serum albumin was studied at different temperatures using fluorescence quenching and synchronous fluorescence methods. The results indicated that aspirin could quench the intrinsic fluorescence of bovine serum albumin through a static quenching process; the electrostatic interaction contributes to the binding reaction between aspirin and bovine serum albumin. The order of magnitude of binding constants was 103, and the primary binding site for aspirin was found to be sub-hydrophobic domain IIA of bovine serum albumin. The results obtained by the two methods were consistent, which indicated synchronous fluorescence spectrometry was a new method of studying the binding mechanism between drug and protein, and it was a useful supplement to the conventional method.