Date of Award

6-2017

Document Type

Open Access

Degree Name

Bachelor of Science

Department

Chemistry

First Advisor

Laura MacManus-Spencer

Language

English

Keywords

chemicals, PFAA, bio-accumulate, protein, protein, dialysis

Abstract

Perfluoroalkyl acids (PFAAs) are industrial chemicals used in everyday products ranging from non-stick coatings to fire-fighting foam. PFAAs are contaminants of emerging concern (CECs) and are bioaccumulative, persistent and toxic. Unlike other CECs, PFAAs bioaccumulate in areas of high protein concentration, such as the kidneys, liver and blood; therefore, it is vital to study PFAA-protein interactions. Human Serum Albumin (HSA) is the model protein used for PFAA-protein studies because it is the most abundant protein in the human body and it binds and transports endogenous and exogenous ligands. Previously, researchers have investigated PFAA-HSA binding, but most of these studies have focused on medium-chain length PFAAs and lacked a systematic method to quantify PFAA-HSA binding. Additionally, few studies have focused on determining a relationship between PFAA chain length and binding strength. In this study, a systematic method was used to determine relationships between PFAA chain length and ionic head group and protein binding; the binding affinities of short-medium- and long-chain PFAAs were determined using a systematic equilibrium dialysis method coupled with liquid chromatography-tandem mass spectrometry. The results indicate that the short-chain PFAAs, depending on ionic head group, bind as strongly or only moderately weaker at the high-affinity sites than the medium- and long-chain PFAAs.

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