Evidence map›Paper›PMID 34450368›Full record

ArticleChemosphere2022

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

Jessica L Alesio, Angela Slitt, Geoffrey D Bothun

Abstract read
In one paragraph

Article in Chemosphere, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. The Impact of Forever Chemicals on Protein Structure and Function.International journal of molecular sciences · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. An in vitro and machine learning framework for quantifying serum albumin binding of per- and polyfluoroalkyl substances.Toxicological sciences : an official journal of the Society of Toxicology · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Jessica L AlesioDepartment of Chemical Engineering, University of Rhode Island, 2 East Alumni Ave, Kingston, RI, 02881, United States.
Angela SlittDepartment of Biomedical and Pharmaceutical Sciences, University of Rhode Island, 7 Greenhouse Rd, Kingston, RI, 02881, United States.
Geoffrey D BothunDepartment of Chemical Engineering, University of Rhode Island, 2 East Alumni Ave, Kingston, RI, 02881, United States. Electronic address: gbothun@uri.edu.

Funding

Sources, Transport, Exposure & Effects of PFAS (STEEP) Center - RENEWALP42ES027706 · NIEHS · UNIVERSITY OF RHODE ISLAND · PI Angela L Slitt · 2017 to 2026
$18.9M
NIEHS NIH HHS P42 ES027706
6 · The paper itself

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.

Indexed as

Alkanesulfonic AcidsEnvironmental PollutantsFluorocarbonsAlbuminsHumansPropionatesAlbuminsAlkanesulfonic AcidsEnvironmental PollutantsFluorocarbonsPropionatesAlbuminEquilibrium dialysisFluorescence quenchingPFASProtein binding

Identifiers

PMID34450368
PMCPMC8612954

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.