Characterization of Binding of Raltegravir to Plasma Proteins | Zendy

Caroline Barau | Zendy; Valérie Furlan | Zendy; Yazdan Yazdanpanah | Zendy; Catherine Fagard | Zendy; JeanMichel Molina | Zendy; AnneMarie Taburet | Zendy; Aurélie BarrailTran | Zendy

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Characterization of Binding of Raltegravir to Plasma Proteins

Author(s) -

Caroline Barau,

Valérie Furlan,

Yazdan Yazdanpanah,

Catherine Fagard,

JeanMichel Molina,

AnneMarie Taburet,

Aurélie BarrailTran

Publication year - 2013

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.00625-13

Subject(s) - raltegravir , ultrafiltration (renal) , plasma protein binding , albumin , chemistry , orosomucoid , binding site , chromatography , serum albumin , blood proteins , glycoprotein , biochemistry , biology , human immunodeficiency virus (hiv) , immunology , viral load , antiretroviral therapy

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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