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
Full text: Unavailable
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.