Thermodynamics of the Interaction of BCBP with Bovine Serum Albumin

Celecoxib derivatives are widely used, non-steroidal, anti-inflammatory drugs for the treatment of acute or chronic inflammation. Under simulated physiological conditions, we used fluorescence and ultraviolet absorption spectroscopy, circular dichroism, and methods of molecular simulation to study the thermodynamics of the interaction between the celecoxib derivative 1-benzenesulfonamides-3-carboxyl-5-phenyl pyrazole (BCBP) and bovine serum albumin (BSA). The fluorescence quenching of BSA by BCBP was a static process, which was confirmed by the UV-Vis absorption spectra. The calculated enthalpy (Delta H) and entropy (Delta S) changes implied that hydrogen bonds and van der Waals forces played a predominant role in the binding process. The circular dichroism demonstrated that the secondary structure of BSA changed after its interaction with BCBP, causing the alpha-helix content to decrease, accompanied by an increase in an unordered structure. Molecular docking results confirmed the experimental results.