Evidence map›Paper›PMID 33550662›Full record

ArticleProtein science : a publication of the Protein Society2021

Unveiling the binding mode of perfluorooctanoic acid to human serum albumin.

Lorenzo Maso, Matteo Trande, Stefano Liberi, Giulia Moro, Elise Daems, Sara Linciano, Frank Sobott, Sonia Covaceuszach, Alberto Cassetta, Silvano Fasolato and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.2field-weighted citation impact, top 5% of its field
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

22 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
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  6. The Impact of Forever Chemicals on Protein Structure and Function.International journal of molecular sciences · 2026
    Review
  7. Article
  8. Article
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  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
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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

14 authors at 5 institutions in 3 countries.

Lorenzo MasoDepartment of Biology, University of Padua, Padova, Italy.ORCID 0000-0002-3380-2902
Matteo TrandeDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Mestre, Italy.ORCID 0000-0002-8602-047X
Stefano LiberiDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Mestre, Italy.ORCID 0000-0003-3858-6919
Giulia MoroDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Mestre, Italy.ORCID 0000-0003-4383-936X
Elise DaemsDepartment of Bioscience Engineering, University of Antwerp, Antwerp, Belgium.ORCID 0000-0003-3910-3149
Sara LincianoDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Mestre, Italy.ORCID 0000-0003-4192-4421
Frank SobottDepartment of Chemistry, University of Antwerp, Antwerp, Belgium.ORCID 0000-0001-9029-1865
Sonia CovaceuszachIstituto di Cristallografia - CNR, Trieste Outstation, Trieste, Italy.ORCID 0000-0001-7453-1099
Alberto CassettaIstituto di Cristallografia - CNR, Trieste Outstation, Trieste, Italy.ORCID 0000-0002-8600-4162
Silvano FasolatoDepartment of Medicine, University of Padua, Padova, Italy.ORCID 0000-0002-5730-2267
Ligia M MorettoDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Mestre, Italy.ORCID 0000-0002-4127-6957
Karolien De WaelDepartment of Bioscience Engineering, University of Antwerp, Antwerp, Belgium.ORCID 0000-0003-4495-0748
Laura CendronDepartment of Biology, University of Padua, Padova, Italy.ORCID 0000-0002-0125-0461
Alessandro AngeliniDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Mestre, Italy.ORCID 0000-0001-5923-3843
Ca' Foscari University of Venice · ITUniversity of Antwerp · BEUniversity of Padua · ITInstitute of Crystallography · ITUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Perfluorooctanoic acid (PFOA) is a toxic compound that is absorbed and distributed throughout the body by noncovalent binding to serum proteins such as human serum albumin (hSA). Though the interaction between PFOA and hSA has been already assessed using various analytical techniques, a high resolution and detailed analysis of the binding mode is still lacking. We report here the crystal structure of hSA in complex with PFOA and a medium-chain saturated fatty acid (FA). A total of eight distinct binding sites, four occupied by PFOAs and four by FAs, have been identified. In solution binding studies confirmed the 4:1 PFOA-hSA stoichiometry and revealed the presence of one high and three low affinity binding sites. Competition experiments with known hSA-binding drugs allowed locating the high affinity binding site in sub-domain IIIA. The elucidation of the molecular basis of the interaction between PFOA and hSA might provide not only a better assessment of the absorption and elimination mechanisms of these compounds in vivo but also have implications for the development of novel molecular receptors for diagnostic and biotechnological applications.

Indexed as

Models, MolecularCaprylatesCrystallography, X-RayFluorocarbonsHumansProtein DomainsSerum Albumin, HumanCaprylatesFluorocarbonsperfluorooctanoic acidSerum Albumin, Humanbinding modecrystal structurefluoroalkyl substanceshuman serum albuminmolecular interactionperfluorooctanoic acid

Identifiers

PMID33550662
PMCPMC7980502
OpenAlexW3126935118

What OpenQuestion holds

Textmetadata
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.