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Stereoselective binding of etodolac to human serum albumin
Author(s) -
Muller Noëlle,
Lapicque Françoise,
Monot Claudine,
Payan Elisabeth,
Dropsy Rémi,
Netter Patrick
Publication year - 1992
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.530040407
Subject(s) - chemistry , etodolac , enantiomer , human serum albumin , albumin , serum albumin , chromatography , plasma protein binding , stereoselectivity , in vitro , stereochemistry , biochemistry , catalysis
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. © 1992 Wiley‐Liss, Inc.