Evidence map›Paper›PMID 19239717›Full record

ArticleBMC molecular biology2009

Binding of PFOS to serum albumin and DNA: insight into the molecular toxicity of perfluorochemicals.

Xian Zhang, Ling Chen, Xun-Chang Fei, Yin-Sheng Ma, Hong-Wen Gao

Open access · hybridAbstract read
In one paragraph

Article in BMC molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
8.6field-weighted citation impact, top 2% 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

32 citing papers in PubMed, 115 citations in OpenAlex.

  1. Trial
  2. Review
  3. Review
  4. The Impact of Forever Chemicals on Protein Structure and Function.International journal of molecular sciences · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Screening Peptide-Binding Partners for GenX via Phage Display.International journal of molecular sciences · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Unveiling the binding mode of perfluorooctanoic acid to human serum albumin.Protein science : a publication of the Protein Society · 2021
    Article
  18. Article
  19. Article
  20. Review
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

5 authors at 3 institutions in 1 country.

Xian ZhangState Key Laboratory of Pollution Control and Resource Reuse, College of Environmental Science and Engineering, Tongji University, Shanghai 200092, PR China. zhangwxian1001@yahoo.com.cn
Ling Chen
Xun-Chang Fei
Yin-Sheng Ma
Hong-Wen Gao
Tongji University · CNNanjing Forestry University · CNState Key Laboratory of Pollution Control and Resource Reuse · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHealth risk from exposure of perfluorochemicals (PFCs) to wildlife and human has been a subject of great interest for understanding their molecular mechanism of toxicity. Although much work has been done, the toxigenicity of PFCs remains largely unknown. In this work, the non-covalent interactions between perfluorooctane sulfonate (PFOS) and serum albumin (SA) and DNA were investigated under normal physiological conditions, aiming to elucidate the toxigenicity of PFCs.

resultsIn equilibrium dialysis assay, the bindings of PFOS to SA correspond to the Langmuir isothermal model with two-step sequence model. The saturation binding number of PFOS was 45 per molecule of SA and 1 per three base-pairs of DNA, respectively. ITC results showed that all the interactions were spontaneous driven by entropy change. Static quenching of the fluorescence of SA was observed when interacting with PFOS, indicating PFOS bound Trp residue of SA. CD spectra of SA and DNA changed obviously in the presence of PFOS. At normal physiological conditions, 1.2 mmol/l PFOS reduces the binding ratio of Vitamin B2 to SA by more than 30%.

conclusionThe ion bond, van der Waals force and hydrophobic interaction contributed to PFOS binding to peptide chain of SA and to the groove bases of DNA duplex. The non-covalent interactions of PFOS with SA and DNA alter their secondary conformations, with the physiological function of SA to transport Vitamin B2 being inhibited consequently. This work provides a useful experimental method for further studying the toxigenicity of PFCs.

Indexed as

Alkanesulfonic AcidsAnimalsBinding SitesBiological TransportDNAElectrolytesFluorescenceFluorocarbonsHumansHydrogen-Ion ConcentrationModels, MolecularProtein BindingProtein Structure, TertiaryRiboflavinSerum AlbuminTemperatureAlkanesulfonic AcidsDNAElectrolytesFluorocarbonsperfluorooctane sulfonic acidRiboflavinSerum AlbuminTryptophan

Identifiers

PMID19239717
PMCPMC2656506
OpenAlexW2101872249

What OpenQuestion holds

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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.