Thermophysical Properties of the Amyloid Beta Protein from Differential Scanning Calorimetry

The amyloid beta (Aβ) protein is thought to play a major role in Alzheimer's Disease. Alzheimer's Disease is a late onset, progressive process associated with Aβ protein deposits and neurofibrillary tangles (Taylor 2003). Alzheimer's Disease is the most prevalent dementia (over 2/3 of all cases) in the developing world and the third leading cause of natural death in the United States (Walsh, 2001). Alzheimer's Disease is one of the amyloid diseases which are characterized by at least twenty proteins that aggregate to form insoluble fibrils with β-sheet secondary structure that affects humans and animals alike (Walsh, 2001). This research presents experimentally determined thermophysical properties such as the enthalpy of reaction, Gibbs free energy, entropy, reaction order, and activation energy using differential scanning calorimetry and predicted values from the van't Hoff equation and direct concentration measurements to better characterize the process of fibril elongation.