Stereoselective binding of etodolac to human serum albumin. |
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Authors: | N Muller F Lapicque C Monot E Payan R Dropsy P Netter |
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Affiliation: | Laboratoire de Pharmacologie, URA CNRS 1288, Faculté de Médecine, Vandoeuvre les Nancy, France. |
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Abstract: | 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. |
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Keywords: | NSAID chirality enantiomers protein binding equilibrium dialysis fluorescent specific markers |
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