title: Enantioselectivity of the binding of (S)- and (R)-7-chloro-1,3-dihydro-3-methyl-5-phenyl-2H-1,4-benzodiazepines to human serum albumin.
abstract: By combining the gel filtration and circular dichroism (CD) methods in studying the binding of chiral (S)/(R)-(I) to human serum albumin (HSA) the following results were obtained: HSA affinity for (S)-(I) is about 17 times higher than for (R)-(I); there exist two independent and nonequivalent binding sites for (S)-(I), and one site of lower affinity for (R)-(I); at equimolar concentrations of (I) and HSA, (S)-enantiomer is bound up to 45%, but (R)-enantiomer binds up to 22% only; differential CD-spectra at various concentrations, in the presence of HSA at 1.45 X 10(-5) M concentration, reveals distortions of the chromophoric system i.e. of the conformation of (S)-(I). This effect, and the low affinity of both enantiomers for HSA, allows only a qualitative interpretation of CD-data.
authors.forename: G
authors.initials: G
authors.lastname: Gratton
authors.forename: E
authors.initials: E
authors.lastname: Decorte
authors.forename: F
authors.initials: F
authors.lastname: Moimas
authors.forename: C
authors.initials: C
authors.lastname: Angeli
authors.forename: V
authors.initials: V
authors.lastname: Sunjić
mesh_terms: D001569:Benzodiazepines / Q000097:blood / Q000378:metabolism*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002850:Chromatography, Gel; D002942:Circular Dichroism; D006801:Humans; D011485:Protein Binding; D011963:Receptors, GABA-A / Q000378:metabolism; D012709:Serum Albumin / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013237:Stereoisomerism
chemical_list: D011963:Receptors, GABA-A; D012709:Serum Albumin; D001569:Benzodiazepines