Protein Regge Trajectories, Phase Coexistence and Physics of Alzheimer's Disease

TL;DR

This paper explores a novel physical process involving phase coexistence of proteins within cells, proposing it as a potential factor in Alzheimer's disease development, which could offer new insights into its underlying mechanisms.

Contribution

It introduces the concept of phase coexistence in intracellular proteins as a possible cause of Alzheimer's, a novel idea in the context of polymer physics and neurodegeneration.

Findings

Proposes phase coexistence as a new factor in Alzheimer's pathology

Suggests intracellular protein instability may contribute to disease onset

Introduces a physical perspective on amyloid precursor protein behavior

Abstract

Alzheimer's disease causes severe neurodegeneration in the brain that leads to a certain death. The defining factor is the formation of extracellular senile amyloid plaques in the brain. However, therapeutic approaches to remove them have not been effective in humans, and so our understanding of the cause of Alzheimer's disease remains incomplete. Here we investigate physical processes that might relate to its onset. Instead of the extracellular amyloid, we scrutinize the intracellular domain of its precursor protein. We argue for a phenomenon that has never before been discussed in the context of polymer physics: Like ice and water together, the intracellular domain of the amyloid precursor protein forms a state 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.