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Alzheimer’s disease and mad cow disease (Creutzfeldt-Jakob disease) are similar in that both are thought to be caused by abnormally folded prion proteins in the brain. It is the accumulation of amyloid fibers created by the abnormal prion proteins that is seen as the cause for Alzheimer’s disease.

James Shorter, PhD, Assistant Professor of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, has made a surprising discovery. A small molecule, called DAPH, can be used to target the areas that hold the amyloid fibers together and convert the fibers to a form that makes them unable to grow. DAPH accomplishes this remarkable goal by preventing growth from the ends of the fibers.

The DAPH molecule remodels the fiber architecture, which is something researchers have not been able to accomplish before. DAPH was originally found in a screen of small molecules that reduce amyloid-beta toxicity by Vernon Ingram, Massachusetts Institute of Technology (MIT), and co-researcher.

When a small amount of amyloid (or prion) fiber is added to the normal form of the protein it is converted to the fiber form. However, when DAPH is added the conversion process is prevented and essentially stops fiber formation in its tracks.

Some types of amyloids may be helpful–like in formation of memories–so, researchers are now looking for a way to selectively choose which type of amyloid protein is affected.