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.

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@article{Zamparo2010SimplifiedES, title={Simplified exactly solvable model for β-amyloid aggregation.}, author={Marco Zamparo and Antonio Trovato and Amos Maritan}, journal={Physical review letters}, year={2010}, volume={105 10}, pages={108102} }