Designing A Bioinspired Degradation System for Forever Chemicals in Water Using Molecular Simulations

Per- and polyfluoroalkyl substances (PFAS), often termed “forever chemicals”, are resistant to natural biodegradation processes. PFAS poses many health risks and environmental challenges and is correlated with causing certain types of cancer, immune system disorders, and pollution. As a result, many approaches have been attempted to degrade PFAS and more similar substances but have been inefficient in degradation because of high cost, producing toxic byproducts, and high energy intensity. This research proposes a method of utilizing the fatty acid photodecarboxylase (5NCC), a photo enzyme that requires light to catalyze its reactions obtained from the Protein Data Bank, to degrade PFAS. Since the molecular characteristics of PFAS are similar to the protein’s natural ligand, palmitic acid (PLM), we suggest that PFAS is also degradable by the fatty acid photodecarboxylase (5NCC) protein. We produced the highest occupied molecular orbitals (HOMO), the lowest occupied molecular orbitals (LUMO), and molecular dynamic (MD) simulations of the 5NCC enzyme with a carboxylate PFAS ligand to assess binding affinity and examine if it can emulate the PLM ligand. These experimentations investigates the efficiency of carboxylate versions of a novel PFAS degradation system and represents a step forward in achieving sustainable solutions for the PFAS contamination global issue.