Noncovalent Interactions of Long-Chain Perfluoroalkyl Acids with Serum Albumin

Bischel, HN; Macmanus-Spencer, LA; Luthy, RG

HERO ID

1279027

Reference Type

Journal Article

Year

2010

Language

English

PMID

20540534

HERO ID 1279027
In Press No
Year 2010
Title Noncovalent Interactions of Long-Chain Perfluoroalkyl Acids with Serum Albumin
Authors Bischel, HN; Macmanus-Spencer, LA; Luthy, RG
Journal Environmental Science & Technology
Volume 44
Issue 13
Page Numbers 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 association constant may be a useful parameter to characterize the bioaccumulative potential and in vivo bioavailability of PFAAs. In this work, association constants (K(a)) 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 10(6) 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 K(PW) > 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 10(5) M(-1) for PFOA and PFNA and 10(4) M(-1) for perfluorodecanoate and perfluorooctanesulfonate. The results reported here suggest binding through specific high affinity interactions at low PFAA:albumin mole ratios.
Doi 10.1021/es101334s
Pmid 20540534
Wosid WOS:000279304700070
Url https://search.proquest.com/docview/609374927?accountid=171501
Is Certified Translation No
Dupe Override No
Comments Source: Web of Science 000279304700070
Is Public Yes
Language Text English
Keyword Environmental Studies; Proteins; Binding sites; Mass spectrometry; Bioavailability
Is Qa No