Prions are infectious protein particles that cause a unique group of fatal neurodegenerative diseases in humans and animals. Unlike bacteria, viruses, fungi, and parasites, prions do not contain nucleic acids such as DNA or RNA. They are composed entirely of an abnormally folded form of a naturally occurring protein known as the prion protein (PrP). The normal cellular form, designated PrP^C, is present mainly in the nervous system and performs important physiological functions. However, when it changes into the abnormal form, designated PrP^Sc, it acquires the ability to convert normal prion proteins into the abnormal form. This chain reaction results in the accumulation of insoluble protein aggregates in the brain. Prion diseases are collectively known as transmissible spongiform encephalopathies (TSEs) because affected brain tissue develops microscopic sponge-like holes due to neuronal degeneration. These diseases are characterized by long incubation periods, progressive neurological impairment, absence of inflammation, and inevitable death. Prions are highly resistant to heat, radiation, ultraviolet light, and many chemical disinfectants that normally destroy microorganisms. Therefore, they pose significant challenges in