Effect of Residue Substitutions on the Hydrophobic Core of the C-Terminus of the Prion Protein

Prion diseases are fatal neurodegenerative that affect mammals, including humans. The hallmark of prion is the protein: misfolded and aggregated form protein PrPSc binds to cellular PrPC induces conformational conversion. Although gene polymorphisms correlate with varying degrees susceptibility host develop diseases, how residue substitutions modulate structural dynamics towards pathological misfolding unknown. Deciphering such mechanism will identify potential druggable hot spots stabilize prevent Our bioinformatics study focuses on effect stability hydrophobic core C-terminal PrPC. We discuss our results in light correlation between domains, increased degree species developing diseases.