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Updated: May 9, 2026

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Published on: May 9, 2025
Characterization of binding of raltegravir to plasma proteins
Caroline Barau1, Valérie Furlan, Yazdan Yazdanpanah
1Assistance Publique, Hôpitaux de Paris, Hôpital Bicêtre, Hôpitaux Universitaires Paris-Sud, Service de Pharmacie Clinique, Paris, France.
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.
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