Stereoselective binding of etodolac to human serum albumin.

N Muller, F Lapicque, C Monot, E Payan, R Dropsy, P Netter

Laboratoire de Pharmacologie, URA CNRS 1288, Faculté de Médecine, Vandoeuvre les Nancy, France.

Chirality 1992

filter terms:

The protein binding of etodolac enantiomers was studied in vitro by equilibrium dialysis in human serum albumin (HSA) of various concentrations varying from 1 to 40 g/liter, by addition of each enantiomer at increasing concentrations. In the 1 g/liter solution, at the lowest drug levels, the (R)-form is more bound than its antipode, the contrary being observed at the highest drug levels. For higher albumin concentrations, S was bound in a larger extent than R. Using the displacement of specific markers of HSA sites I and II, studied by spectrofluorimetry, it was suggested that R and S are both bound to site I, while only S is strongly bound to site II.