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2007 Grant - Turner

Drug-Protein Complexes as Inhibitors of Beta-Amyloid Aggregation

Raymond Scott Turner, M.D., Ph.D.
University of Michigan
Ann Arbor, Michigan

2007 Investigator-Initiated Research Grant

Any protein in the body must "fold" itself into its correct three-dimensional shape in order for it to carry out its function properly. In Alzheimer's disease, some proteins — including the protein fragment beta-amyloid — undergo an unchecked chemical change that results in misfolding. These structural changes cause them to lose their normal function and enable them to form abnormal structures that may become toxic to brain cells.

One potential treatment strategy to correct problems with misfolded proteins is to enhance the function of chaperone proteins. Chaperones help other proteins assume their correct shape, stabilize correctly folded proteins, correct misfolded proteins or mediate the degradation of misfolded proteins.

For their proposed study, Raymond Scott Turner, M.D., Ph.D., and colleagues will engineer drug-like molecules that can direct chaperones to prevent beta-amyloid from assembling into strutures that are toxic to brain cells. The team will conduct their studies using cell cultures.

Results from this research could lay the groundwork for similar efforts using mice genetically altered to produce Alzheimer-like symptoms. Ultimately, Dr. Turner's work could lead to the development of novel therapies for Alzheimer's disease and other neurodegenerative disorders involving misfolded proteins.