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American Society for Microbiology, Antimicrobial Agents and Chemotherapy, 11(64), 2020

DOI: 10.1128/aac.00895-20

Authorea, 2020

DOI: 10.22541/au.158636268.80439895

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Characteristics of Dolutegravir and Bictegravir Plasma Protein Binding: A First Approach for the Study of Pharmacologic Sanctuaries

This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Data provided by SHERPA/RoMEO

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.