Binding of pirprofen to human serum albumin studied by dialysis and spectroscopy techniques.

The interaction of pirprofen with human serum albumin (HSA) was investigated by equilibrium dialysis and spectroscopic (UV absorption, fluorescence, CD, NMR) techniques. It was found that HSA binds pirprofen nonstereospecifically. The binding of pirprofen depends upon the N-B conformational change of albumin. Chloride ions appear to displace the drug from its binding site. The thermodynamic parameters suggest that the interaction may be explained by electrostatic as well as hydrophobic forces. The absorption spectral changes which accompanied the binding of pirprofen to HSA implied that the aromatic portion of drugs was inserted into the hydrophobic crevice in the protein, while the carboxyl group of the drug interacted with a cationic site on the albumin surface. The NMR data indicated that the pyrroline ring and propionic acid parts may be the major binding site for HSA. A specific binding site for pirprofen on the HSA was found to be site II, benzodiazepine site, using fluorescence probes and drug markers. In addition, from the binding data with modified HSA, it seems that Tyr-411 is specifically involved in pirprofen binding.