Author:
Barau Caroline,Furlan Valérie,Yazdanpanah Yazdan,Fagard Catherine,Molina Jean-Michel,Taburet Anne-Marie,Barrail-Tran Aurélie
Abstract
ABSTRACTThe 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 ann(number of sites) ·Kaproduct of 9.8 × 102liters/mol. A pH increase of 0.2 U led to a 2% increase in the bound fraction.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
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