Evidence map›Paper›PMID 36148994›Full record

ArticleChemical research in toxicology2022

Investigation of the Interaction between Human Serum Albumin and Branched Short-Chain Perfluoroalkyl Compounds.

Giulia Moro, Stefano Liberi, Filippo Vascon, Sara Linciano, Sofia De Felice, Silvano Fasolato, Carlo Foresta, Luca De Toni, Andrea Di Nisio, Laura Cendron and 1 more

Abstract read
In one paragraph

Article in Chemical research in toxicology, 2022. 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
–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

22 citing papers in PubMed.

  1. Article
  2. Review
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  4. Bioaccumulation of PFOS Isomers in Transporter Proteins.Chemical research in toxicology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. 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
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

11 authors.

Giulia MoroDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Via Torino 155, 30172 Venice, Italy.
Stefano LiberiDepartment of Biology, University of Padua, Viale G. Colombo 3, 35131 Padua, Italy.
Filippo VasconDepartment of Biology, University of Padua, Viale G. Colombo 3, 35131 Padua, Italy.
Sara LincianoDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Via Torino 155, 30172 Venice, Italy.
Sofia De FeliceDepartment of Biology, University of Padua, Viale G. Colombo 3, 35131 Padua, Italy.
Silvano FasolatoDepartment of Medicine, University of Padua, Via Giustiniani 2, 35128 Padua, Italy.
Carlo ForestaDepartment of Medicine, Unit of Andrology and Reproductive Medicine, University of Padua, Via Giustiniani 2, 35128 Padua, Italy.
Luca De ToniDepartment of Medicine, Unit of Andrology and Reproductive Medicine, University of Padua, Via Giustiniani 2, 35128 Padua, Italy.
Andrea Di NisioDepartment of Medicine, Unit of Andrology and Reproductive Medicine, University of Padua, Via Giustiniani 2, 35128 Padua, Italy.
Laura CendronDepartment of Biology, University of Padua, Viale G. Colombo 3, 35131 Padua, Italy.
Alessandro AngeliniDepartment of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Via Torino 155, 30172 Venice, Italy.ORCID 0000-0001-5923-3843

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The current trend dealing with the production of per- and polyfluoroalkyl substances (PFASs) involves the shifting toward branched short-chain fluorinated compounds known as new-generation PFASs. A key aspect to be clarified, to address the adverse health effects associated with the exposure to PFASs, is their binding mode to human serum albumin (hSA), the most abundant protein in plasma. In this study, we investigated the interaction between hSA and two representative branched short-chain PFASs, namely, HPFO-DA and C6O4. In-solution studies revealed that both compounds bind hSA with affinities and stoichiometries lower than that of the legacy long-chain perfluoroalkyl compound PFOA. Competition experiments using hSA-binding drugs with known site-selectivity revealed that both HPFO-DA and C6O4 bound to pockets located in subdomain IIIA. The crystal structure of hSA in complex with HPFO-DA unveiled the presence of two binding sites. The characterization and direct comparison of hSA interactions with new-generation PFASs may be key elements for the understanding of the toxicological impact of these compounds.

Indexed as

Alkanesulfonic AcidsFluorocarbonsBinding SitesHumansSerum Albumin, HumanAlkanesulfonic AcidsFluorocarbonsSerum Albumin, Human

Identifiers

PMID36148994
PMCPMC9682524

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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.