Critical new insights into the binding of poly- and perfluoroalkyl substances (PFAS) to albumin protein

Alesio, Jessica L.; Slitt, Angela; Bothun, Geoffrey D.

doi:10.1016/j.chemosphere.2021.131979

Cited by 91Per- and polyfluoroalkyl substances researchProtein Interaction Studies and Fluorescence AnalysisFluorine in Organic Chemistry

Critical new insights into the binding of poly- and perfluoroalkyl substances (PFAS) to albumin protein

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Alesio, Jessica L., Slitt, Angela, Bothun, Geoffrey D.·2022·Chemosphere

DOI 10.1016/j.chemosphere.2021.131979PMC PMC8612954

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Abstract

With an increasing number of health-related impacts of per- and polyfluoroalkyl substances (PFAS) being reported, there is a pressing need to understand PFAS transport within both the human body and the environment. As proteins can serve as a primary transport mechanism for PFAS, understanding PFAS binding to proteins is essential for predictive physiological models where accurate values of protein binding constants are vital. In this work we present a critical analysis of three common models for analyzing PFAS binding to bovine serum albumin (BSA) based on fluorescence quenching: the Stern-Volmer model, the modified Stern-Volmer model, and the Hill equation. The PFAS examined include perfluorooctanoic acid (PFOA), perfluorononanoic acid (PFNA), perfluorodecanoic acid (PFDA), perfluorobutanesulfonic acid (PFBS), perfluorohexanesulfonic acid (PFHxS), perfluorooctanesulfonic acid (PFOS), and the replacement compound 2,3,3,3-tetrafluoro-2-(heptafluoropropoxy)propanoate (HFPO-DA or GenX). While all three models capture the general effects of hydrophobicity and steric limitations to PFAS binding, the Hill equation highlighted a unique relationship between binding cooperativity and the number of fluorinated carbons, with PFOA exhibiting the greatest binding cooperativity. The significance of steric limitations was confirmed by comparing results obtained by fluorescence quenching, which is an indirect method based on specific binding, to those obtained by equilibrium dialysis where PFAS binding directly correlated with traditional measures of hydrophobicity. Finally, the binding constants were correlated with PFAS physicochemical properties where van der Waals volume best described the steric limitations observed by fluorescence quenching.

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Cooperative binding models have linked and predicted protein associations using conventional hydrophobicity measures and their influence on biomacromolecule interactions.
“Cooperative binding models have further correlated (and predicted) protein associations, relying on traditional measures of hydrophobicity and its effect on biomacromolecule interactions (124).”
From Per- and polyfluoroalkyl substances in the environment (2022) · cites this paper as [124]
The Results and Discussion sections report that the Hill model accounts for cooperativity in PFAS–albumin binding and that binding constants correlate with log Kow, a measure of hydrophobicity (pages not specified in our copy). They do not show that a cooperative model predicted protein associations from hydrophobicity alone; the paper also identifies steric effects as important. (LLM, conf=0.84)
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Differential scanning fluorimetry to assess PFAS binding to bovine serum albumin protein
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Authors: Alesio, J. L., Slitt, A., & Bothun, G. D.
Affiliations: University of Rhode Island (US)
Corresponding author: Bothun, Geoffrey D.
ORCID: Alesio, Jessica L.
Slitt, Angela
Bothun, Geoffrey D.
Venue: Chemosphere
Publisher: Elsevier BV
Published: 2022-01
Volume: 287
Issue: Pt 1
Pages: 131979
ISSN: 0045-6535 (ISSN-L)
DOI: 10.1016/j.chemosphere.2021.131979
PMC: PMC8612954
OpenAlex: W3195727434
Semantic Scholar: de4d9a01e7e2b268e07f48376dae7260d9608c6e
Cited by: 91
References: 37
Citations by year: 2026: 14 · 2025: 26 · 2024: 23 · 2023: 17 · 2022: 11
FWCI: 4.81
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (am, 235 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Chemosphere (acceptedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Journal of Media Literacy Education (submittedVersion, cc-by)
Funders: National Institute of Environmental Health Sciences (P42ES027706)
Topics: Physical Sciences › Environmental Science › Environmental Chemistry › Per- and polyfluoroalkyl substances research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmaceutical Science › Fluorine in Organic Chemistry
Keywords: per- and polyfluoroalkyl substances, PFAS, bovine serum albumin, protein binding, binding constant, fluorescence quenching, Stern-Volmer model, Hill equation, cooperative binding, hydrophobicity, van der Waals volume, perfluorooctanoic acid, PFOS, GenX, perfluorinated carboxylic acids, perfluorinated sulfonic acids, equilibrium dialysis, PFAS transport
MeSH terms: Albumins, Environmental Pollutants, Fluorocarbons, Humans, Propionates, Alkanesulfonic Acids

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Critical new insights into the binding of poly- and perfluoroalkyl substances (PFAS) to albumin protein

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