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  • Title: Oligomerization of amyloid Abeta16-22 peptides using hydrogen bonds and hydrophobicity forces.
    Author: Favrin G, Irbäck A, Mohanty S.
    Journal: Biophys J; 2004 Dec; 87(6):3657-64. PubMed ID: 15377534.
    Abstract:
    The 16-22 amino-acid fragment of the beta-amyloid peptide associated with the Alzheimer's disease, Abeta, is capable of forming amyloid fibrils. Here we study the aggregation mechanism of Abeta16-22 peptides by unbiased thermodynamic simulations at the atomic level for systems of one, three, and six Abeta16-22 peptides. We find that the isolated Abeta16-22 peptide is mainly a random coil in the sense that both the alpha-helix and beta-strand contents are low, whereas the three- and six-chain systems form aggregated structures with a high beta-sheet content. Furthermore, in agreement with experiments on Abeta16-22 fibrils, we find that large parallel beta-sheets are unlikely to form. For the six-chain system, the aggregated structures can have many different shapes, but certain particularly stable shapes can be identified.
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