title: Stereoselective binding of etodolac to human serum albumin.
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.
authors.affiliation: Laboratoire de Pharmacologie, URA CNRS 1288, Faculté de Médecine, Vandoeuvre les Nancy, France.
authors.forename: N
authors.initials: N
authors.lastname: Muller
authors.forename: F
authors.initials: F
authors.lastname: Lapicque
authors.forename: C
authors.initials: C
authors.lastname: Monot
authors.forename: E
authors.initials: E
authors.lastname: Payan
authors.forename: R
authors.initials: R
authors.lastname: Dropsy
authors.forename: P
authors.initials: P
authors.lastname: Netter
mesh_terms: D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000378:metabolism*; D001665:Binding Sites; D003956:Dialysis; D017308:Etodolac / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013237:Stereoisomerism
chemical_list: D000894:Anti-Inflammatory Agents, Non-Steroidal; D012709:Serum Albumin; D017308:Etodolac