title: The existence of conformationally labile (preformed) drug binding sites in human serum albumin as evidenced by optical rotation measurements.
abstract: The ability of certain drugs to induce conformational changes in human serum albumin has been examined by differential optical rotation measurements at 233 nm. At drug:protein molar ratios ([D]/[P]) of unity, the optical rotation increased, decreased or remained the same depending on the drug used. The change in the optical rotatory dispersion (ORD) signal was investigated as a function of the drug concentration. Drug-protein interactions were relatively specific. There exists at least one, and possibly more, stable preformed high affinity sites for the binding of drugs to albumin. At low [D]/[P] ratios, the ORD titration curves suggest that the high affinity sites are conformationally labile and that the albumin molecule is flexible.
authors.affiliation: Department of Pharmacy, King's College, London, UK.
authors.forename: F
authors.initials: F
authors.lastname: Walji
authors.forename: A
authors.initials: A
authors.lastname: Rosen
authors.forename: R C
authors.initials: RC
authors.lastname: Hider
mesh_terms: D001665:Binding Sites; D002740:Chlorothiazide / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D009904:Optical Rotation; D004364:Pharmaceutical Preparations / Q000378:metabolism*; D010600:Pharmacology; D011485:Protein Binding; D011487:Protein Conformation / Q000187:drug effects; D012709:Serum Albumin / Q000378:metabolism*
chemical_list: D004364:Pharmaceutical Preparations; D012709:Serum Albumin; D002740:Chlorothiazide