The pathogenic conversion of prion protein (PrPC) is one of the most representative examples of a natively folded protein that in response to detrimental stimuli may acquire aggregation propensity, form fibril deposits, and ultimately cause neurodegenerative disorders [1, 2] The misfolded or “scrapie” isoform (PrPSc) has been identified as the major component of prions: the infectious entities of transmissible spongiform encephalopathy (TSE) [3, 4]. This evidence concerns the gene PRNP and human prion disease.