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3856523 
Journal Article 
Development of a fluorescence model for the binding of medium- to long-chain perfluoroalkyl acids to human serum albumin through a mechanistic evaluation of spectroscopic evidence 
Hebert, PC; Macmanus-Spencer, LA 
2010 
Yes 
Analytical Chemistry
ISSN: 0003-2700
EISSN: 1520-6882 
82 
15 
6463-6471 
English 
A novel model for measuring the strength of perfluoroalkyl acid (PFAA) binding to human serum albumin (HSA) by use of the protein's native fluorescence is described. The model is derived from published properties of HSA and its interactions with other surfactants; it is consistent with these properties and experimental observations. The model's validity has been tested with both medium- to long-chain PFAAs (perfluoroheptanoate, perfluorooctanoate, perfluorononanoate, perfluorodecanoate, perfluoroundecanoate, perfluorohexanesulfonate, and perfluorooctanesulfonate) and short-chain PFAAs (perfluorohexanoate and perfluorobutanesulfonate). These experiments confirm the model as a valid description for the binding of medium- to long-chain PFAAs to HSA. Results indicate at least 2-3 PFAAs bind to each protein with affinity on the order of 10(4) M(-1). These binding strengths exhibit a dependence on protein concentration. Measured PFAA binding constants are approximately 10% of those values reported for fatty acids of similar chain length; correcting for protein concentration suggests the binding strengths may be as low as 2-3% of the corresponding fatty acids' affinities. Like fatty acids, the carboxylate PFAAs exhibit a trend of generally increasing binding strength with increased chain length. The model does not appear valid for the binding of short-chain PFAAs to HSA. Hill binding coefficients, fluorescence intensity measurements, and wavelengths of maximum emission suggest short-chain PFAAs associate with HSA differently and fail to promote the same conformational changes in the protein's tertiary structure as the medium- to long-chain PFAAs. 
Chemistry--Analytical Chemistry; Fluorescence; Proteins; Binding sites; Fatty acids; Surfactants; Molecular structure; Analytical chemistry 
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