Characterization of binding of raltegravir to plasma proteins.

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Barau C, Furlan V, Yazdanpanah Y, Fagard C, Molina JM, Taburet AM, Barrail-Tran A

Characterization of binding of raltegravir to plasma proteins.

Antimicrob Agents Chemother. 2013 Oct;57(10):5147-50. doi: 10.1128/AAC.00625-13. Epub 2013 Jul 15.

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23856784 [ View in PubMed
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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 x 10(2) liters/mol. A pH increase of 0.2 U led to a 2% increase in the bound fraction.

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