Protein Pairing and Lipid Linking: Physicochemical Properties of Poly- and Perfluoroalkyl Substances (PFAS) Influence Their Interactions with Macromolecules
Poly- and perfluoroalkyl substances (PFAS) are a growing class of synthetic compounds used in a wide variety commercial and residential applications due to their hydrophobic and oleophobic properties. Since this body of work began, the list of the number of PFAS has grown from 1,000 to over 4,200. As this number increases, there is a pressing need to quickly understand a) if certain PFAS are harmful to humans and the environment and b) how harmful each compound is. The objective of this work was to characterize PFAS binding to proteins and lipid bilayers. Better understanding of these mechanisms aids in future work regarding predicting overall risk of certain PFAS. The focus in this work was on evaluating common models used to quantify the binding of ligands to proteins, development of a high throughput screening technique to quantify PFAS-protein binding, and characterizing PFAS binding to two different lipid bilayers. It was determined that a combination of chain length, logKOW (an indicator of hydrophobicity), and van der Waals volume (a measure of molecular size), play crucial roles in PFAS interaction with macromolecules.