In Silico Screening of SNP's in Prion Protein and Comparative Studies between Phytochemical Compounds that inhibit Prion Protein Causing Neuro-degenerative Diseases

The misfolded PrP (prion protein) aggregates and deposits in the brain as a sign of neurodegenerative diseases, which are very lethal. The prion-like prionoids lead to a variety of neurodegenerative diseases in humans as well as in animals. Prion protein is active in the brain and several other tissues which are made by receiving instructions from the PRNP gene. Prion diseases are progressive, fatal, attack the brain structure or additional neural cells, and lack effective treatment. Consequently, there is an imperative need to create new and more effective remedial strategies needs to combat these fatal diseases. The current work aim is to identify mutated SNP and its position which is responsible for the main cause of the disease. We have predicted the protein stability, Amino acid function, Secondary structure of the amino acid,
Mutated prion protein Homology modeling, and analysis of Protein 3D structure. Through the literature survey, we have identified phytochemical compounds from medicinal plants which possess pharmacological activities to cure neurodegenerative diseases. And we have also
retrieved a few currently used synthetic compounds which are used for the treatment of neurodegenerative disease. Both the set of compounds were further analyzed for Molecular docking against the target prion protein. The docking results and comparative docking studies
reveal that the natural compounds exhibit the best binding energy than the synthetic compounds. Natural compounds are more effective in the treatment and cure of various neurodegenerative diseases without any side effects.