Project DetailsA protein called amyloid precursor protein (APP) can be cut into toxic and non‐toxic forms of beta‐amyloid. The toxic forms of beta‐amyloid (called beta‐amyloid 42) misfold and clump together into brain plaques, a hallmark of Alzheimer's disease. Other beta‐amyloid fragments of APP do not misfold. Dr. Peter Tessier and collaborators will use new detection methods to study the differences between toxic and non‐toxic folding of beta‐amyloid proteins in Alzheimer's disease. Their long term goal is to design a drug that could prevent this folding and clumping. If successful, this method could be applied to toxic misfolding that happens in other neurodegenerative diseases, like Parkinson's disease, Huntington's disease, and Prion disease (including Creutzfeld‐Jacob or “Mad Cow” disease).