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Oligomerization of Amyloid Aß_16–22 Peptides Using Hydrogen Bonds and Hydrophobicity Forces

Complex Systems Division, Department of Theoretical Physics, Lund University, Lund, Sweden

Correspondence: Address reprint requests to A. Irbäck, Tel: 46-46-222-3493; Fax: 46-46-222-9686; E-mail: anders{at}thep.lu.se.

The 16–22 amino-acid fragment of the ß-amyloid peptide associated with the Alzheimer's disease, Aß, is capable of forming amyloid fibrils. Here we study the aggregation mechanism of Aß_16–22 peptides by unbiased thermodynamic simulations at the atomic level for systems of one, three, and six Aß_16–22 peptides. We find that the isolated Aß_16–22 peptide is mainly a random coil in the sense that both the -helix and ß-strand contents are low, whereas the three- and six-chain systems form aggregated structures with a high ß-sheet content. Furthermore, in agreement with experiments on Aß_16–22 fibrils, we find that large parallel ß-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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