Your browser has javascript turned off or blocked. This will lead to some parts of our website to not work properly or at all. Turn on javascript for best performance.

The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Anders Irbäck. Photo.

Anders Irbäck

Professor

Anders Irbäck. Photo.

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
  • Department of Astronomy and Theoretical Physics

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