Amyloids are made of a collection of small protein monomers. These monomers tend to be of proteins that are intrinsically disordered in an alternative, but energetically favorable conformation. Once this conformation has taken place the protein secondary structure is typically rich in beta sheets and this conformation allows the monomers to create amyloid fibrils. These fibrils are seen in a number of diseases including, but not limited to Alzheimer's, Parkinson's, and Huntington's disease. It has been estimated that in the year 2050 all major diseases causing fatalities will be decreased, but amyloid diseases will actually increase. It has been shown that plant and herbal extracts are able to block the aggregation of amyloid fibrils containing amyloid-beta (associated with Alzheimer's) in vitro. Some proteins that are able to form amyloids have been termed prions because they have been shown to be infectious in organisms that are amyloid free. These include fatal familial insomnia, bovine spongiform encephalopathy (mad cow disease), and chronic wasting disease (CWD). The proteins that cause these diseases are all called PrP and vary only slightly from species to species. It was observed that the CWD epidemic amongst deer was limited to those that were not eating lichens in North American forests. This implies that lichens have some sort of chemical that is able to block the aggregation or cure amyloid disease. The ability of a chemical from a lichen extract has yet to successfully block or cure amyloid aggregation in vitro. Using a variety of lichens, many of which would be in the diets of deer, it is possible to find a natural blocking or curing agent using the prion Sup35. Sup35 is a yeast prion and aggregates very similarly to PrP and other amyloids.

Possible lichen extracts as a blocking agent of Sup35 amyloids

248th National Meeting (2014)

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