title: The fatty-acid-induced conformational states of human serum albumin investigated by means of multiple co-binding of protons and oleic acid.
abstract: The binding of oleic acid to human serum albumin causes progressive changes in (a) the pK of some amino acid residues, as detected by pH-stat titration and (b) the induced molar ellipticities of albumin-bound drugs (diazepam and oxyphenbutazone), as measured by c.d. It is concluded that albumin undergoes several conformational transitions as the amount of oleic acid bound increases from 0 to about 9 molecules/molecule of protein. At least three different conformations of the protein seem to be involved. These conformations can be linked with the three classes of oleic acid-binding sites on albumin.
authors.affiliation: Department of Pharmaceutical Chemistry, Faculty of Pharmacy, State University of Utrecht, The Netherlands.
authors.forename: J H
authors.initials: JH
authors.lastname: Dröge
authors.forename: L H
authors.initials: LH
authors.lastname: Janssen
authors.forename: J
authors.initials: J
authors.lastname: Wilting
mesh_terms: D001665:Binding Sites; D002942:Circular Dichroism; D003975:Diazepam / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D019301:Oleic Acid; D009829:Oleic Acids / Q000494:pharmacology*; D010113:Oxyphenbutazone / Q000378:metabolism; D011487:Protein Conformation / Q000187:drug effects; D011522:Protons; D012709:Serum Albumin / Q000378:metabolism*
chemical_list: D008024:Ligands; D009829:Oleic Acids; D011522:Protons; D012709:Serum Albumin; D019301:Oleic Acid; D010113:Oxyphenbutazone; D003975:Diazepam