| Literature DB >> 32868324 |
Thibaut Gelé1,2, Hélène Gouget2, Valérie Furlan3, Pierre-Hadrien Becker4, Anne-Marie Taburet2, Olivier Lambotte2,5,6, Aurélie Barrail-Tran7,2,8.
Abstract
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.Entities:
Keywords: bictegravir; dolutegravir; human alpha-1-acid glycoprotein; human serum albumin; pharmacokinetics; protein binding
Year: 2020 PMID: 32868324 PMCID: PMC7577134 DOI: 10.1128/AAC.00895-20
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191