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Photo of Anders Irbäck

Anders Irbäck

Professor

Photo of Anders Irbäck

Oligomerization of amyloid A beta(16-22) peptides using hydrogen bonds and hydrophobicity forces

Author

  • Giorgio Favrin
  • Anders Irbäck
  • Sandipan Mohanty

Summary, in English

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 Abeta(16-22) peptides by unbiased thermodynamic simulations at the atomic level for systems of one, three, and six Abeta(16-22) peptides. We find that the isolated Abeta(16-22) 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 Abeta(16-22) 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.

Department/s

  • Computational Biology and Biological Physics - Has been reorganised
  • Department of Astronomy and Theoretical Physics - Has been reorganised

Publishing year

2004

Language

English

Pages

3657-3664

Publication/Series

Biophysical Journal

Volume

87

Issue

6

Document type

Journal article

Publisher

Cell Press

Topic

  • Biophysics

Status

Published

ISBN/ISSN/Other

  • ISSN: 1542-0086