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• W1980141451 abstract "Abstract Interactions of perfluoroalkyl acids (PFAAs) with tissue and serum proteins likely contribute to their tissue distribution and bioaccumulation patterns. Protein–water distribution coefficients ( K PW ) based on ligand associations with bovine serum albumin (BSA) as a model protein were recently proposed as biologically relevant parameters to describe the environmental behavior of PFAAs, yet empirical data on such protein binding behavior are limited. In the present study, associations of perfluoroalkyl carboxylates (PFCAs) with two to 12 carbons (C 2 –C 12 ) and perfluoroalkyl sulfonates with four to eight carbons (C 4 , C 6 , and C 8 ) with BSA are evaluated at low PFAA:albumin mole ratios and various solution conditions using equilibrium dialysis, nanoelectrospray ionization mass spectrometry, and fluorescence spectroscopy. Log K PW values for C 4 to C 12 PFAAs range from 3.3 to 4.3. Affinity for BSA increases with PFAA hydrophobicity but decreases from the C 8 to C 12 PFCAs, likely due to steric hindrances associated with longer and more rigid perfluoroalkyl chains. The C 4 ‐sulfonate exhibits increased affinity relative to the equivalent chain‐length PFCA. Fluorescence titrations support evidence that an observed dependence of PFAA‐BSA binding on pH is attributable to conformational changes in the protein. Association constants determined for perfluorobutanesulfonate and perfluoropentanoate with BSA are on the order of those for long‐chain PFAAs ( K a ∼10 6 /M), suggesting that physiological implications of strong binding to albumin may be important for short‐chain PFAAs. Environ. Toxicol. Chem. 2011;30:2423–2430. © 2011 SETAC" @default.
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• W1980141451 date "2011-09-14" @default.
• W1980141451 modified "2023-10-16" @default.
• W1980141451 title "Strong associations of short-chain perfluoroalkyl acids with serum albumin and investigation of binding mechanisms" @default.
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• W1980141451 doi "https://doi.org/10.1002/etc.647" @default.
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