ChBE Seminar Series: Theresa Good

Friday, October 12, 2012
10:00 a.m.-11:00 a.m.
Room 2110 Chemical and Nuclear Engineering Bldg.
Professor Jeffery B. Klauda

Engineering New Strategies for the Treatment of Alzheimer's Disease

Theresa Good
Department of Chemical, Biochemical & Environmental Engineering
University of Maryland, Baltimore County

Alzheimer’s disease is the leading cause of dementia in the aging population, affecting close to 30 million people world wide. One of the histopathological hallmarks of Alzheimer’s disease is the deposition of insoluble protein in the form of senile plaques. The primary protein component of these plaques is β-amyloid, a 39 to 43 amino acid peptide which is able to self assemble into amyloid fibrils. It is hypothesized by many that the deposition of aggregated β-amyloid (in fibril, protofibril, or oligomer form) is associated with neurotoxicity in the diseases. In our laboratory, we are interested in understanding how this protein takes on its characteristic amyloid structure, how size and structure are related to toxicity, and the interactions between the protein and cells that lead to toxicity. To that end we have developed complementary experimental and modeling approaches based on traditional chemical engineering analysis to gain insights into mechanisms of disease and the role of protein structure in disease. Results from this work including computational protein-ligand docking, FRET analysis of potential β-amyloid receptor interactions, chemical modification and hydrogen exchange coupled with mass spectrometry to examine protein structure, and development of biomimtic materials to prevent β-amyloid-cell interactions will be discussed. We have also begun to explore why stem cell therapies don’t work in Alzheimer’s disease. Some very preliminary results on this topic will be presented.

Audience: Graduate  Faculty  Post-Docs 


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