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Binding of Perfluorocarboxylates to Serum Albumin: A Comparison of Analytical Methods

MacManus-Spencer, Laura A ; Tse, Monica L ; Hebert, Paul C ; Bischel, Heather N ; Luthy, Richard G

Analytical chemistry (Washington), 2010-02, Vol.82 (3), p.974-981 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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Título:
Binding of Perfluorocarboxylates to Serum Albumin: A Comparison of Analytical Methods
Autor: MacManus-Spencer, Laura A ; Tse, Monica L ; Hebert, Paul C ; Bischel, Heather N ; Luthy, Richard G
Assuntos: Analytical chemistry ; Animals ; Binding sites ; Caprylates - chemistry ; Cattle ; Chemistry ; Chlorofluorocarbons ; Comparative analysis ; Decanoic Acids - chemistry ; Exact sciences and technology ; Fluorescence ; Fluorocarbons - chemistry ; General, instrumentation ; Humans ; Lauric Acids - chemistry ; Magnetic Resonance Spectroscopy - methods ; Protein Binding ; Proteins ; Serum Albumin - chemistry ; Serum Albumin, Bovine - chemistry ; Spectrometric and optical methods ; Spectrometry, Fluorescence - methods ; Spectrum analysis
É parte de: Analytical chemistry (Washington), 2010-02, Vol.82 (3), p.974-981
Descrição: Perfluorochemicals are globally pervasive contaminants that are persistent, bioaccumulative, and toxic. Perfluorocarboxylic acids (PFCAs) with 8−13 carbons accumulate in the liver and blood of aquatic organisms; PFCA−protein interactions may explain this accumulation pattern. Here, the interactions between PFCAs with 8−11 carbons and serum albumin are examined using three experimental approaches: surface tension titrations, 19F NMR spectroscopy, and fluorescence spectroscopy. Surface tension titrations indicate complex formation at high (mM) PFCA concentrations. Secondary association constants ranging from 102 to 104 M−1 were determined from 19F NMR titrations at high PFCA:albumin mole ratios. Fluorescence measurements indicate that PFCA−albumin interactions alter the protein conformation at low PFCA:albumin mole ratios (up to 5:1) and suggest two binding classes with association constants around 105 and 102 M−1. While 19F NMR and fluorescence provide both qualitative and quantitative information about PFCA−albumin interactions, surface tension provides only qualitative information. Limitations associated with instrumentation and methods require high PFCA concentrations in both surface tension and 19F NMR experiments; in contrast, fluorescence allows for analysis of a wider range of PFCA concentrations and PFCA:albumin mole ratios. Results from this study indicate that fluorescence, though an indirect method, offers a more comprehensive picture of the nature of PFCA−albumin interactions.
Editor: Washington, DC: American Chemical Society
Idioma: Inglês

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Binding of Perfluorocarboxylates to Serum Albumin: A Comparison of Analytical Methods

MacManus-Spencer, Laura A ; Tse, Monica L ; Hebert, Paul C ; Bischel, Heather N ; Luthy, Richard G

Washington, DC: American Chemical Society

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