Stereoselective protein binding of ketoprofen: Effect of albumin concentration and of the biological system

✍ Scribed by Nathalie Dubois; Françloise Lapicque; Michel Abiteboul; Dr. Patrick Netter

• Publisher: John Wiley and Sons
• Year: 1993
• Tongue: English
• Weight: 758 KB
• Volume: 5
• Category: Article
• ISSN: 0899-0042
• DOI: 10.1002/chir.530050305

✦ Synopsis

Equilibrium dialysis was used to study in vitro the enantioselective binding of R, S, and racemic ketoprofen at physiological pH and temperature in human serum albumin (HSA) (1, 20, and 40 g/liter) and in plasma. The binding of enantiomers in a racemic mixture was studied to see the effect of each isomer on the other's interaction with the protein. The free fractions were determined by high-performance liquid chromatography. The binding of ketoprofen enantiomers to albumin was enantioselective, depending on both drug and protein concentrations. Enantioselectivity was observed in plasma too but was the opposite of that in HSA at 40 g/liter. The percentage of each isomer unbound was higher in the racemic mixture than with the isomer alone. The displacement of probes specific for HSA sites I and 11, studied by spectrofluorimetry, suggests that all three preparations of ketoprofen are bound