title: Characterization of binding of raltegravir to plasma proteins.
abstract: The objective of this study was to characterize raltegravir (RAL) binding to albumin and alpha-1-acid glycoprotein (AAG). Unbound and bound RAL were separated by ultrafiltration. The association constant (Ka) was estimated by a graphical method. In HIV-infected patients, the average plasma protein binding is 76%. RAL did not bind to AAG but bound to nonsaturable, low-affinity albumin sites with an n (number of sites) · Ka product of 9.8 × 10(2) liters/mol. A pH increase of 0.2 U led to a 2% increase in the bound fraction.
authors.affiliation: Assistance Publique, Hôpitaux de Paris, Hôpital Bicêtre, Hôpitaux Universitaires Paris-Sud, Service de Pharmacie Clinique, Paris, France.
authors.forename: Caroline
authors.initials: C
authors.lastname: Barau
authors.forename: Valérie
authors.initials: V
authors.lastname: Furlan
authors.forename: Yazdan
authors.initials: Y
authors.lastname: Yazdanpanah
authors.forename: Catherine
authors.initials: C
authors.lastname: Fagard
authors.forename: Jean-Michel
authors.initials: JM
authors.lastname: Molina
authors.forename: Anne-Marie
authors.initials: AM
authors.lastname: Taburet
authors.forename: Aurélie
authors.initials: A
authors.lastname: Barrail-Tran
mesh_terms: D001798:Blood Proteins / Q000737:chemistry*; D006801:Humans; D009961:Orosomucoid / Q000737:chemistry; D011485:Protein Binding; D011760:Pyrrolidinones / Q000737:chemistry*; D000068898:Raltegravir Potassium
chemical_list: D001798:Blood Proteins; D009961:Orosomucoid; D011760:Pyrrolidinones; D000068898:Raltegravir Potassium