Polyoxometalates Mediated Amyloid Fibrillation Dynamics and Restoration of Enzyme Activity of Hen Egg White Lysozyme Treated under Cold Atmospheric Pressure Plasma

Neurodegenerative disorders are one of the most devastating disorders worldwide. Although a definite mechanistic pathway of neurodegenerative disorders is still not clear, it is almost clear that these diseases are initiated by protein misfolding. Hen Egg White Lysozyme (Lyz) can be converted to highly arranged amyloid fibrils and is therefore considered a good model protein for studying protein aggregation in connection to neurodegeneration. In this study, Lyz has been converted to fibrils using He-air gas fed single jet cold atmospheric plasma (CAP). The reactive oxygen species and the reactive nitrogen species produced by the plasma jet interact with the protein molecules and enhance the fibril formation. We monitored the fibrillation kinetics with the Thioflavin T (ThT) assay and observed that fibrils are formed when the samples are treated for 10 min with He-air gas fed CAP. Further, we studied the role of a special class of inorganic nanomaterials called polyoxometalates (POMs) in the process of the Lyz fibrillation using various biophysical techniques. The Keggin POMs used in this study are phosphomolybdic acid (PMA) and silico molybdic acid (SMA). Keggin POMs bring in structural self-assembly of the protein and disrupt the fibrils as evidenced in the ThT assay and TEM analysis. Molecular docking studies together with electrokinetic potential studies show the interactions between POMs and Lyz dominated via hydrogen bonding and electrostatic interactions. The enzyme activity of Lyz was assessed using the substrate Micrococcus lysodeikticus and after treatment with POMs results showed a significant increase in the activity. This study could pave way for looking into Keggin POMs for possible application in neurodegeneration.