Dominant entropic binding of perfluoroalkyl substances (PFASs) to albumin protein revealed by ¹⁹F NMR.

ABSTRACT: Mechanistic insight into protein binding by poly- and perfluoroalkyl substances (PFASs) is critical to understanding how PFASs distribute and accumulate within the body and to developing predictive models within and across classes of PFASs. Fluorine nuclear magnetic resonance spectroscopy (¹⁹F NMR) has proven to be a powerful, yet underutilized tool to study PFAS binding; chemical shifts of each fluorine group reflect the local environment along the length of the PFAS molecule. Using bovine serum albumin (BSA), we report dissociation constants, K_d, for four common PFASs well below reported critical micelle concentrations (CMCs) - perfluorooctanoic acid (PFOA), perfluorononanoic acid (PFNA), perfluorohexanesulfonic acid (PFHxS), and perfluorooctanesulfonic acid (PFOS) 

SUBMITTER: Fedorenko M 

PROVIDER: S-EPMC8479757 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature