Prion proteins can undergo a refolding (or misfolding) toward an alternative, highly cooperative polymeric conformational state, which is able to self-replicate by serving as a structural model or template for the soluble molecules of the protein ( prion (proteinaceous infectious particle) emerges from the biomedical field as the causative agent of several neurodegenerative diseases, known as transmissible spongiform encephalopathies or TSEs (i.e., bovine Scrapie, bovine Spongiform Encephalopathy or mad cow disease, and human Creutzfeldt-Jakob disease and Kuru) (Prusiner, 1982
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