Open AccessCharacteristics of Dolutegravir and Bictegravir Plasma Protein Binding: a First Approach for the Study of Pharmacologic Sanctuaries
Author(s) -
Thibaut Gelé,
Hélène Gouget,
Valérie Furlan,
Pierre-Hadrien Becker,
AnneMarie Taburet,
Olivier Lambotte,
Aurélie Barrail-Tran
Publication year - 2020
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.00895-20
Subject(s) - dolutegravir , human serum albumin , plasma protein binding , in vitro , chemistry , binding site , glycoprotein , albumin , serum albumin , biochemistry , virology , biology , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load
This study aimed to characterize in vitro dolutegravir (DTG) and bictegravir (BIC) binding. They had a preferential binding to human serum albumin (HSA) with two classes of albumin sites. Human alpha-1-acid glycoprotein (HAAG) binding of DTG and BIC showed an atypical nonlinear binding. The low-affinity site on HSA, the main plasma binding protein, suggests that the high protein binding rate should not impair passive diffusion.