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• W1995919892 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 association constant may be a useful parameter to characterize the bioaccumulative potential and in vivo bioavailability of PFAAs. In this work, association constants (Ka) and binding stoichiometries for PFAA-albumin complexes are quantified over a wide range of PFAA:albumin mole ratios. Primary association constants for perfluorooctanoate (PFOA) or perfluorononanoate (PFNA) with the model protein bovine serum albumin (BSA) determined via equilibrium 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 physiological PFAA:albumin mole ratio (<10−3), corresponding to a high protein-water distribution coefficient (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. Association constants estimated 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." @default.
• W1995919892 created "2016-06-24" @default.
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• W1995919892 date "2010-06-11" @default.
• W1995919892 modified "2023-10-16" @default.
• W1995919892 title "Noncovalent Interactions of Long-Chain Perfluoroalkyl Acids with Serum Albumin" @default.
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• W1995919892 doi "https://doi.org/10.1021/es101334s" @default.
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