Molecular polymorphism of Aβ in Alzheimer's disease

Abstract 

Alzheimer's disease is defined pathologically by the presence of senile plaques, which consist primarily of extracellular aggregates of fibrillar Aβ peptide, and neurofibrillary tangles, which are abnormal, intracellular bundles of fibrillar tau protein. The advent of amyloid binding agents as diagnostic imaging probes for Alzheimer's disease (AD) has made it imperative to understand at a molecular and disease level what these ligands are reporting. In addition to improving the accuracy of diagnosis, we argue that these selective ligands can serve as probes for molecular polymorphisms that may govern the pathogenicity of abnormal protein aggregates.

Keywords: PIB, Transgenic mice, Stoichiometry, High affinity binding, Thioflavine T, Congo Red, Polythiophene