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

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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
DOI 10.1186/1471-2199-10-16PMC PMC2656506
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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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Figures

Figure 1 Plots of (A) γ vs. cL0 and (B) γ-1 vs. cL-1 for the PFOS solutions containing 0.02 mmol/l SA (1) and 0.96 mmol/l DNA (2) at pH7.40 at 37°C in the presence of 0.15 mol/l NaCl.
Figure 1 Plots of (A) γ vs. cL0 and (B) γ-1 vs. cL-1 for the PFOS solutions containing 0.02 mmol/l SA (1) and 0.96 mmol/l DNA (2) at pH7.40 at 37°C in the presence of 0.15 mol/l NaCl.CC BY · PubMed Central
Figure 2 Effects of pH (A), electrolyte (B) and temperature (C) on γ of solutions containing 0.8 mmol/l PFOS, 0.016 mmol/l SA (A and B) and 0.02 mmol/l SA (C), 0.9 mmol/l DNA (A) and 1.19 mmol/l DNA (B and C).
Figure 2 Effects of pH (A), electrolyte (B) and temperature (C) on γ of solutions containing 0.8 mmol/l PFOS, 0.016 mmol/l SA (A and B) and 0.02 mmol/l SA (C), 0.9 mmol/l DNA (A) and 1.19 mmol/l DNA (B and C).CC BY · PubMed Central
Figure 3 (A) The fluorescence spectra of solutions containing 0.5 μmol/l SA and variable PFOS from 1 to 8: 0, 2.5, 5, 7.5, 10, 12.5, 15, 17.5 μmol/l at pH7.40. (B) Plot of F0/F vs. Q for the SA-PFOS solutions.
Figure 3 (A) The fluorescence spectra of solutions containing 0.5 μmol/l SA and variable PFOS from 1 to 8: 0, 2.5, 5, 7.5, 10, 12.5, 15, 17.5 μmol/l at pH7.40. (B) Plot of F0/F vs. Q for the SA-PFOS solutions.CC BY · PubMed Central
Figure 4 The molar ellipticity CD curves of solutions containing (A) 0.4 μmol/l SA in the presence of PFOS from 1 to 5: 0, 16, 20, 24, 40 μmol/l and (C) 100 μmol/l DNA with PFOS from 1 to 4: 0, 20, 30, 40 μmol/l; (B) Plot of fraction (%) vs. C0, PFOS for the SA-PFOS solutions. All solutions were prepared at pH7.40.
Figure 4 The molar ellipticity CD curves of solutions containing (A) 0.4 μmol/l SA in the presence of PFOS from 1 to 5: 0, 16, 20, 24, 40 μmol/l and (C) 100 μmol/l DNA with PFOS from 1 to 4: 0, 20, 30, 40 μmol/l; (B) Plot of fraction (%) vs. C0, PFOS for the SA-PFOS solutions. All solutions were prepared at pH7.40.CC BY · PubMed Central
Figure 5 ITC titration curves of (A) PFOS-SA and (B) PFOS-DNA interactions at pH7.40. The temperature was 37°C. The experiment was conducted by injecting: 2.5 mmol/l PFOS (10 μl every time) into the ITC cell (1.4685 ml) containing (A) 0.01 mmol/l SA or (B) 0.5 mmol/l DNA. The titration profile was integrated and corrected for the heat of dilution, which was estimated by a separate experiment by injecting the PFOS into the B-R buffer. The corrected heat was divided by the moles of injectant, and values were plotted as a function of the PFOS/SA and PFOS/DNA molar ratio. The titration curve was fitted by a nonlinear least squares method.
Figure 5 ITC titration curves of (A) PFOS-SA and (B) PFOS-DNA interactions at pH7.40. The temperature was 37°C. The experiment was conducted by injecting: 2.5 mmol/l PFOS (10 μl every time) into the ITC cell (1.4685 ml) containing (A) 0.01 mmol/l SA or (B) 0.5 mmol/l DNA. The titration profile was integrated and corrected for the heat of dilution, which was estimated by a separate experiment by injecting the PFOS into the B-R buffer. The corrected heat was divided by the moles of injectant, and values were plotted as a function of the PFOS/SA and PFOS/DNA molar ratio. The titration curve was fitted by a nonlinear least squares method.CC BY · PubMed Central
Figure 6 Cartoon illustrating the possible binding sites of PFOS in SA (A) and DNA (B).
Figure 6 Cartoon illustrating the possible binding sites of PFOS in SA (A) and DNA (B).CC BY · PubMed Central
Figure 7 Effect of PFOS on the physiological function of SA to transport VB2. All solutions contained 0.02 mmol/l SA and 0.04 mmol/l VB2 at pH 7.40 at 37 °C in the presence of 0.15 mol/l NaCl.
Figure 7 Effect of PFOS on the physiological function of SA to transport VB2. All solutions contained 0.02 mmol/l SA and 0.04 mmol/l VB2 at pH 7.40 at 37 °C in the presence of 0.15 mol/l NaCl.CC BY · PubMed Central
Figure 8 The device designed for equilibrium dialysis. (1) – semi-permeable membrane with 12.5 ml of dialysate; (2) – the temperature sensor for maintaining the reaction at constant 37°C; (3) – Dialysis solution 37.5 ml; (4) – water bath at constant 37°C. The apparatus was placed on a thermostated magnetic stirrer (5) and rotary magnets were used to mix solutions (3) and (4) thoroughly. The PFOS concentration in solution (3) was determined from the sampling tube (6).
Figure 8 The device designed for equilibrium dialysis. (1) – semi-permeable membrane with 12.5 ml of dialysate; (2) – the temperature sensor for maintaining the reaction at constant 37°C; (3) – Dialysis solution 37.5 ml; (4) – water bath at constant 37°C. The apparatus was placed on a thermostated magnetic stirrer (5) and rotary magnets were used to mix solutions (3) and (4) thoroughly. The PFOS concentration in solution (3) was determined from the sampling tube (6).CC BY · PubMed Central
Figure 9 (A) Working curve for determination of PFOS between 0 and 1.60 mmol/l according to the dialysis procedures at pH 7.40 in 0.15 mol/l NaCl and the detection method with CPC and ECR, measured at 626 nm. (B) Effect of dialysis time on recovery of PFOS in the mother liquor containing 0.40 mmol/l PFOS at pH 7.40 in 0.15 mol/l NaCl.
Figure 9 (A) Working curve for determination of PFOS between 0 and 1.60 mmol/l according to the dialysis procedures at pH 7.40 in 0.15 mol/l NaCl and the detection method with CPC and ECR, measured at 626 nm. (B) Effect of dialysis time on recovery of PFOS in the mother liquor containing 0.40 mmol/l PFOS at pH 7.40 in 0.15 mol/l NaCl.CC BY · PubMed Central

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Research works printed but not linked: 1

  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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Metadata

Authors
Zhang, X., Chen, L., Fei, X.-C., Ma, Y.-S., & Gao, H.-W.
Affiliations
  • Tongji University (CN)
  • Nanjing Forestry University (CN)
ORCID
Venue
BMC Molecular Biology
Publisher
Springer Science and Business Media LLC
Published
2009-02-25
Volume
10
Issue
1
Pages
16-16
ISSN
1471-2199 (ISSN-L)
DOI
10.1186/1471-2199-10-16
PMC
PMC2656506
OpenAlex
W2101872249
Semantic Scholar
1e21dbc36a772a1385895e7e1c28276e014b4919
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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