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  • Title: Stereoselective binding of etodolac to human serum albumin.
    Author: Muller N, Lapicque F, Monot C, Payan E, Dropsy R, Netter P.
    Journal: Chirality; 1992; 4(4):240-6. PubMed ID: 1389961.
    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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