Binding of perfluorinated fatty acids to serum proteins

@article{Jones2003BindingOP,
  title={Binding of perfluorinated fatty acids to serum proteins},
  author={Paul D. Jones and Wenyue Hu and Wim M. De Coen and John Newsted and John P. Giesy},
  journal={Environmental Toxicology and Chemistry},
  year={2003},
  volume={22}
}
Perfluorooctane sulfonic acid (PFOS) accumulates in the liver and blood of exposed organisms. The potential for these surfactant molecules to interfere with hormone/protein interactions in blood is of concern given the importance of these interactions. The PFOS binding to serum proteins was investigated by assessing its ability to displace a variety of steroid hormones from specific binding proteins in the serum of birds and fishes. Perfluorooctane sulfonic acid had only a weak ability to… 

Noncovalent interactions of long-chain perfluoroalkyl acids with serum albumin.

The results reported here suggest binding through specific high affinity interactions at low PFAA:albumin mole ratios.

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Routine pharmacochemical models may be applicable to predicting the protein‐based bioaccumulation of long‐chain PFCAs and a comparison of their chemical and physical properties with other well‐studied biologically relevant chemicals showed that accumulation of P FCAs in proteins as the neutral species is predictable.

Identification of perfluorooctane sulfonate binding protein in the plasma of tiger pufferfish Takifugu rubripes.

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References

SHOWING 1-10 OF 39 REFERENCES

Interactions of fluorochemicals with rat liver fatty acid-binding protein.

In vitro data presented in this study support the hypothesis that these fluorochemicals may interfere with the binding of fatty acids or other endogenous ligands to L-FABP and provide evidence to support the hypotheses that displacement of endogenous ligand from L- FABP may contribute to toxicity in rodents fed these fluorochemistryicals.

Binding of the General Anesthetics Propofol and Halothane to Human Serum Albumin

It is shown that the intravenous anesthetic propofol binds at two discrete sites on HSA in preformed pockets that have been shown to accommodate fatty acids, and that the inhalational agent halothane binds at three sites that are also fatty acid binding loci.

Interactions between human plasma sex hormone-binding globulin and xenobiotic ligands

Transport of steroid hormones: interaction of 70 drugs with testosterone-binding globulin and corticosteroid-binding globulin in human plasma.

The results indicate that binding to steroid transport proteins should be considered among the in vivo effects of drugs on endogenous steroid hormone levels.

Accumulation of perfluorooctane sulfonate in marine mammals.

The occurrence of PFOS in marine mammals from the Arctic waters suggests widespread global distribution ofPFOS including remote locations.

Subchronic toxicity studies on perfluorooctanesulfonate potassium salt in cynomolgus monkeys.

Comparison of serum PFOS concentrations associated with no adverse effect in this study to those reported in human blood samples indicated an adequate margin of safety.

Characteristics of the binding of corticosteroid-binding globulin to rat cell membranes.

Specific binding sites for corticosteroid-binding globulin (CBG) were detected on membranes prepared from rat spleen, and electrophoretic patterns from uterine, pulmonary, and renal membranes showed that the less mobile band of the normal CBG doublet appeared to be metabolized to a greater extent than the more mobile band.

Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin.

A crystallographic study of five HSA-fatty acid complexes formed using saturated medium-chain and long-chain fatty acids reveals key similarities and significant differences in the modes of binding, and serves to rationalise much of the biochemical data on fatty acid interactions with albumin.