Protein Regge Trajectories, Phase Coexistence and Loop Aetiology in Alzheimers Disease

Abstract

Alzheimer's disease has a devastating impact on its victims by causing severe neurodegeneration in the brain that leads to a certain death. Only in a small number of cases can the origin be traced to a variety of genetic mutations, for the greater part the reasons for its onset are unclear.The defining factor is the formation of extracellular senile amyloid plaques in the brain, but therapeutic approaches to remove them remain to be shown effective in humans. Here we investigate physical processes that are involved in the release of the extracellular amyloid, by scrutinizing the intracellular domain of its precursor protein. We identify a phenomenon that has never before been discussed in the context of protein research: Like ice and water together, the intracellular domain of the amyloid precursor protein can form a complex of phase coexistence with another protein. This leads to an inherent instability that could well be among the missing pieces in the puzzle of Alzheimer's disease.