Laura MacManus-Spencer - Binding of Perfluorocarboxylates to Serum Albumin: A Comparison of Analytical Methods.

Document created by Laura MacManus-Spencer on Aug 22, 2014
Version 1Show Document
  • View in full screen mode

  Publication Details (including relevant citation   information): MacManus-Spencer, Laura A., Tse, Monica   L., Hebert, Paul C., Bischel, Heather N., Luthy, Richard G.,   Anal. Chem. (Washington, DC, U. S.),   2010, 82 (3), pp 974-981

  Abstract: Perfluorochems. 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 examd. using three exptl. approaches: surface tension   titrns., 19F NMR spectroscopy, and fluorescence spectroscopy.   Surface tension titrns. indicate complex formation at high (mM)   PFCA concns. Secondary assocn. consts. ranging from 102 to 104   M-1 were detd. from 19F NMR titrns. 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   assocn. consts. around 105 and 102 M-1. While 19F NMR and   fluorescence provide both qual. and quant. information about   PFCA-albumin interactions, surface tension provides only qual.   information. Limitations assocd. with instrumentation and methods   require high PFCA concns. in both surface tension and 19F NMR   expts.; in contrast, fluorescence allows for anal. of a wider   range of PFCA concns. 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. [on SciFinder(R)]

  Address (URL):

 

Attachments

    Outcomes