Cited by 119Per- and polyfluoroalkyl substances researchProtein Interaction Studies and Fluorescence AnalysisProtein Structure and Dynamics

Binding of PFOS to Serum Albumin and DNA: Insight into the Molecular Toxicity of Perfluorochemicals

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Zhang, Xian, Chen, Ling, Fei, Xun-Chang, Ma, Yin-Sheng, Gao, Hong-Wen·2009·BMC Molecular Biology

Abstract

BACKGROUND: Health 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. RESULTS: In 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%. CONCLUSION: The 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.

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  1. Yi PG, Yu QS, Shang ZC, Guo M: Study on the interaction between chlortetracycline and bovine serum albumin. Chinese Journal Chemical Physics. 2003, 16: 420-425.

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Authors
Zhang, X., Chen, L., Fei, X.-C., Ma, Y.-S., & Gao, H.-W.
Affiliations
  • Tongji University (CN)
  • Nanjing Forestry University (CN)
Venue
BMC Molecular Biology
Published
2009-02-25
Volume
10
Issue
1
Pages
16-16
ISSN
1471-2199 (ISSN-L)
OpenAlex
W2101872249
Cited by
119
References
82
Citations by year
2026: 7 · 2025: 10 · 2024: 9 · 2023: 3 · 2022: 4 · 2021: 9 · 2020: 10 · 2019: 6 · 2018: 3 · 2017: 1 · 2016: 4 · 2015: 6 · 2014: 12 · 2013: 4 · 2012: 11
FWCI
7.85
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • BMC Molecular Biology (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Topics
  • Physical Sciences › Environmental Science › Environmental Chemistry › Per- and polyfluoroalkyl substances research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
PFOS, perfluorochemicals, serum albumin, DNA binding, molecular toxicity, non-covalent interactions, binding isotherms, entropy-driven binding, tryptophan binding, protein secondary structure, hydrophobic interactions, van der Waals interactions
MeSH terms
Animals, Binding Sites, Biological Transport, DNA, Electrolytes, Fluorescence, Fluorocarbons, Humans, Hydrogen-Ion Concentration, Models, Molecular, Protein Binding, Riboflavin, Serum Albumin, Temperature, Thermodynamics, Tryptophan, Protein Structure, Tertiary, Alkanesulfonic Acids

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