Rapid Characterization of Human Serum Albumin Binding for Per- and Polyfluoroalkyl Substances Using Differential Scanning Fluorimetry.
alcohols
carboxylic acids
fluorocarbons
perfluorocarbons
protein
sulfonic acids
telomer
thermal stability
toxicokinetic
Journal
Environmental science & technology
ISSN: 1520-5851
Titre abrégé: Environ Sci Technol
Pays: United States
ID NLM: 0213155
Informations de publication
Date de publication:
21 09 2021
21 09 2021
Historique:
pubmed:
9
9
2021
medline:
2
10
2021
entrez:
8
9
2021
Statut:
ppublish
Résumé
Per- and polyfluoroalkyl substances (PFAS) are a diverse class of synthetic chemicals that accumulate in the environment. Many proteins, including the primary human serum transport protein albumin (HSA), bind PFAS. The predictive power of physiologically based pharmacokinetic modeling approaches is currently limited by a lack of experimental data defining albumin-binding properties for most PFAS. A novel thermal denaturation assay was optimized to evaluate changes in the thermal stability of HSA in the presence of increasing concentrations of known ligands and a structurally diverse set of PFAS. Assay performance was initially evaluated for fatty acids and HSA-binding drugs ibuprofen and warfarin. Concentration-response relationships were determined and dissociation constants (
Identifiants
pubmed: 34495656
doi: 10.1021/acs.est.1c01200
pmc: PMC8651256
mid: NIHMS1758024
doi:
Substances chimiques
Alkanesulfonic Acids
0
Carboxylic Acids
0
Fluorocarbons
0
Sulfonic Acids
0
Serum Albumin, Human
ZIF514RVZR
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
12291-12301Subventions
Organisme : NIEHS NIH HHS
ID : P30 ES025128
Pays : United States
Organisme : NIEHS NIH HHS
ID : P42 ES031009
Pays : United States
Organisme : NIEHS NIH HHS
ID : T32 ES007046
Pays : United States
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