At the 2008 Days of Molecular Modeling Conference in Sweden, biomedical researcher Trevor Marshall sat on the edge of his chair listening intently to a talk presented by Adriano Aguzzi of the University Hospital of Zurich. Aguzzi was discussing research that confirmed much of what Marshall had long suspected to be true about prions - small, potentially infectious molecules that are hypothesized to be made only of protein.

The protein structure of a prion.

Prions have been implicated as the cause of a number of diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as “mad cow disease”) in cattle, and Creutzfeldt-Jakob disease (CJD) in humans. All thus-far hypothesized prion diseases affect the structure of the brain or other neural tissue, and all are considered untreatable or fatal by mainstream medicine.

Although prions have been studied to some extent in the lab for decades, very little research has delved into their actions when inside the human body (in vivo). Thus, many theories put forth about how prions might cause or contribute to neurological disease have been largely speculative.

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