PFASs are composed of uncomplicated alkyl chains in which hydrogen atoms are substituted with fluoride atoms, resulting in robust carbon-fluorine bonds that are resistant to degradation. These chemicals have strong persistence and bioaccumulation in the environment, with longer chains demonstrating more persistence than shorter ones. Due to their high physicochemical stability, these substances are widely used in many consumer products such as disposable food and toy packaging, apparel, carpeting, and cookware. The primary source of long-term human & domestic cattle exposure to pervasive flame-causing compounds (PFAS) is runoff into nearby rivers from manufacturing industries, airports, and military installations. This is because we do not yet have the necessary infrastructure in place to filter these persistent chemicals out of consumer water. Phosphorylation plays a critical role in the regulation of many cellular processes including cell cycle, growth, apoptosis, and signal transduction pathways which are crucial for the overall life of domestic cows. Phosphorylation is the most common mechanism of regulating protein function and transmitting signals throughout the cell.
In this project, we characterized PFAS-protein binding using ESI-MS techniques and explored their binding mechanism employing molecular docking, MD simulations, sitemap analysis, MM-PBSA, and FEL analysis.
MD Simulation in DESMOND showing Protein-PFAS interactions