Presentation: 2025 ND EPSCoR Annual conference 

October 21, 2025, NDSU Memorial Union, Fargo, North Dakota

Protein–PFAS Interactions: Adsorption and Sensing Potential of Ovalbumin

Per- and polyfluoroalkyl substances (PFAS) pose serious environmental and health challenges, demanding effective sensing and remediation strategies. This study examined ovalbumin (OVA), the predominant protein in egg white (>50% of total protein), as a bio-adsorbent and potential fluorescent sensor for PFAS in water. A combined experimental and computational approach was used to investigate interactions between OVA and seven chemically diverse PFAS compounds. Experimental findings revealed that binding depended on the PFAS chain length. PFAS binding also caused structural changes in OVA. Longer-chain and sulfonate-based PFAS showed stronger binding, mainly through hydrophobic interactions. Molecular docking and molecular dynamics simulations supported these results. These results identified arginine and lysine as important binding sites and showed that fluorination and headgroup chemistry also affect binding. Thermodynamic analysis confirmed favorable binding, with negative enthalpy (ΔH) and free energy (ΔG). The stability of OVA as an adsorbent was further evaluated across varying conditions. In addition, OVA was utilized as a carbon source to prepare fluorescent carbon dots (CDs) through a one-pot hydrothermal synthesis. The resulting fluorescent CDs demonstrated stable physical properties, favorable optical features, and strong potential as fluorescent probes for PFAS detection. Together, these results establish OVA not only as an effective medium for aqueous PFAS adsorption but also as a sustainable platform for the development of fluorescence-based PFAS sensing systems.