A simplified exactly solvable model for beta-amyloid aggregation

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.

4 pages, 2 figures

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Cited by in corpus (5)

• The multiphysics of prion-like diseases: progression and atrophy
• Large Deviations in Renewal Models of Statistical Mechanics
• Fibril elongation mechanisms of HET-s prion-forming domain: Topological evidence for growth polarity
• Finite-size corrections and scaling for the dimer model on the checkerboard lattice
• Statistical Mechanical Treatments of Protein Amyloid Formation