A simplified exactly solvable model for beta-amyloid aggregation

TL;DR

This paper introduces an exactly solvable statistical mechanical model for beta-amyloid aggregation, capturing thermodynamics and phase behavior, and aligning qualitatively with experimental fibril formation data.

Contribution

It presents a novel simplified model that explicitly includes monomer concentration and peptide degrees of freedom, extending previous protein folding models.

Findings

Model reproduces qualitative features of fibril formation

Phase diagram aligns with experimental observations

Incorporates microscopic peptide details

Abstract

We propose an exactly solvable simplified statistical mechanical model for the thermodynamics of beta-amyloid aggregation, generalizing a well-studied model for protein folding. The monomer concentration is explicitly taken into account as well as a non trivial dependence on the microscopic degrees of freedom of the single peptide chain, both in the alpha-helix folded isolated state and in the fibrillar one. The phase diagram of the model is studied and compared to the outcome of fibril formation experiments which is qualitatively reproduced.