Laura MacManus-Spencer - Noncovalent Interactions of Long-Chain Perfluoroalkyl Acids with Serum Albumin.

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  Publication Details (including relevant citation   information): Bischel, Heather N., MacManus-Spencer,   Laura A., Luthy, Richard G., Environ. Sci. Technol.,   2010, 44 (13), pp 5263-5269

  Abstract: Preferential distribution of   long-chain perfluoroalkyl acids (PFAAs) in the liver, kidney, and   blood of organisms highlights the importance of PFAA-protein   interactions in PFAA tissue distribution patterns. A serum   protein assocn. const. may be a useful parameter to characterize   the bioaccumulative potential and in vivo bioavailability of   PFAAs. Assocn. consts. (Ka) and binding stoichiometries for   PFAA-albumin complexes are quantified over a wide range of   PFAA:albumin mole ratios. Primary assocn. consts. for   perfluorooctanoate (PFOA) or perfluorononanoate (PFNA) with the   model protein bovine serum albumin (BSA) detd. via equil.   dialysis are on the order of 106 M-1 with one to three primary   binding sites. PFNA was greater than 99.9% bound to BSA or human   serum albumin (HSA) at a physiol. PFAA:albumin mole ratio   (<10-3), corresponding to a high protein-water distribution   coeff. (log KPW >4). Nanoelectrospray ionization mass   spectrometry (nanoESI-MS) data reveal PFAA-BSA complexes with up   to eight occupied binding sites at a 4:1 PFAA:albumin mole ratio.   Assocn. consts. estd. by nanoESI-MS are on the order of 105 M-1   for PFOA and PFNA and 104 M-1 for perfluorodecanoate and   perfluorooctanesulfonate. The results reported here suggest   binding through specific high affinity interactions at low   PFAA:albumin mole ratios. [on SciFinder(R)]

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