Simplified exactly solvable model for β-amyloid aggregation.

We propose an exactly solvable simplified statistical mechanical model for the thermodynamics of β-amyloid aggregation, generalizing a well-studied model for protein folding. The monomer concentration is explicitly taken into account as well as a nontrivial dependence on the microscopic degrees of freedom of the single peptide chain, both in the α-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.