Detecting Oligomeric Beta-Amyloid for the Diagnosis of Alzheimer’s Disease by Taylor Brownlee A Thesis Presented in the Partial Fulfillment of the Requirements for the Degree Master of Science Approved April 2013 by the Graduate Supervisory Committee: Michael Sierks, Chair

The popular amyloid hypothesis states that beta-amyloid protein aggregates to form sticky deposits in the brain tissue, causing Alzheimer’s disease. Current research studies propose that oligomeric morphologies of beta-amyloid are the principal pathogenic form of the protein. Through the use of a highly-specified capture enzyme-linked immunosorbent assay, the relative quantity of beta-amyloid oligomers was determined in triplicate for a total of 16 transgenic (TG) and nontransgenic (NTG) mice aged five, nine, and thirteen months. A significant p-value of 0.000212 was found between the TG and NTG five month mice. As the age of the TG mice increased, the relative quantity of beta-amyloid oligomers decreased. This suggests that the beta-amyloid oligomers were aggregating to form beta-amyloid fibrils. Conversely, as the age of the NTG mice increased, the quantity of beta-amyloid oligomers increased. This finding supports previous studies that have shown the production of beta-amyloid oligomers in normal aging.