Evidence map›Paper›PMID 41748002›Full record

ArticleEnvironmental research2026

A molecular and cellular understanding of PFDA-exposure-associated outcomes on biological assemblies.

Daisy L Wilson, Sayantani Chakraborty, Ummy Habiba Sweety, Hamidreza Sharifan, Jose A Hernandez, Jason C White, Lela Vukovic, Mahesh Narayan

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Environmental research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Daisy L WilsonEnvironmental Science and Engineering, The University of Texas at El Paso, El Paso, TX, 79968, USA.
Sayantani ChakrabortyDepartment of Chemistry and Biochemistry, The University of Texas at El Paso, El Paso, TX, 79968, USA.
Ummy Habiba SweetyEnvironmental Science and Engineering, The University of Texas at El Paso, El Paso, TX, 79968, USA.
Hamidreza SharifanDepartment of Chemistry and Biochemistry, The University of Texas at El Paso, El Paso, TX, 79968, USA.
Jose A HernandezDepartment of Chemistry and Biochemistry, The University of Texas at El Paso, El Paso, TX, 79968, USA.
Jason C WhiteThe Connecticut Agricultural Experiment Station, New Haven, CT, 06511, USA.
Lela VukovicDepartment of Chemistry and Biochemistry, The University of Texas at El Paso, El Paso, TX, 79968, USA; Computational Science Program, The University of Texas at El Paso, El Paso, TX, 79968, USA; Bioinformatics Program, The University of Texas at El Paso, El Paso, TX, 79968, USA. Electronic address: Lvukovic@utep.edu.
Mahesh NarayanDepartment of Chemistry and Biochemistry, The University of Texas at El Paso, El Paso, TX, 79968, USA. Electronic address: mnarayan@utep.edu.

Funding

UTEP Border Biomedical Research CenterU54MD007592 · NIMHD · UNIVERSITY OF TEXAS EL PASO · PI Marc B Cox · 2019 to 2026
$35.1M
Development and testing of Carbon Quantum Dot architectures to arrest neurotoxicant-insult- related outcomesR16GM145575 · NIGMS · UNIVERSITY OF TEXAS EL PASO · PI NARAYAN, MAHESH · 2022 to 2025
$769k
NIGMS NIH HHS R16 GM145575NIMHD NIH HHS U54 MD007592
6 · The paper itself

Abstract

Human exposure to the fluorosurfactant perfluorodecanoic acid (PFDA) is associated with toxic health outcomes in part arising compromised immune responses. However, the molecular mechanisms leading to adverse physiological outputs have remained elusive. Here, the interactions between PFDA and the milk protein β-lactoglobulin (BLG) was extensively investigated. Our results reveal that PFDA perturbs protein structure in a dose-dependent manner. Furthermore, by binding to BLG (Kd ≈ 3.2 μM; ΔG = -7.5 kcal/mol) PFDA compromises the ability of the protein to recruit and bind to retinol (Vitamin A), which is otherwise transported by lipocalin. This feature was experimentally verified by measuring the kinetics of retinol binding to BLG which was attenuated in the presence of PFDA. Docking and molecular dynamics (MD) simulations expose several intermolecular interactions between the protein-side chain and both the fluoroalkyl tail and polar head group of PFDA providing an understanding of the mechanism(s) by which PFDA competes with retinol binding and also interferes with protein structure. These interactions include salt-bridge formation between the -COO

Indexed as

Decanoic AcidsFluorocarbonsLactoglobulinsAnimalsCaenorhabditis elegansHumansMolecular Docking SimulationMolecular Dynamics SimulationProtein BindingVitamin ADecanoic AcidsFluorocarbonsLactoglobulinsperfluorodecanoic acidVitamin AMolecular modelingPerfluorodecanoic acidProtein-structure-function

Identifiers

PMID41748002
PMCPMC13577653

What Socratic 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 Socratic graph.