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.
Zamparo
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Dipartimento di Fisica G. Galilei and CNISM, Università di Padova, v. Marzolo 8, PD-35131 Padova, Italy. marco.zamparo@pd.infn.it
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Maritan
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D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism; D019277:Entropy; D008958:Models, Molecular; D017510:Protein Folding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary
D016229:Amyloid beta-Peptides