Advanced

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

Favrin, Giorgio LU ; Irbäck, Anders LU and Mohanty, Sandipan LU (2004) In Biophysical Journal 87(6). p.3657-3664
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 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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biophysical Journal
volume
87
issue
6
pages
3657 - 3664
publisher
Cell Press
external identifiers
  • wos:000225426700006
  • pmid:15377534
  • scopus:10044227276
ISSN
1542-0086
DOI
10.1529/biophysj.104.046839
language
English
LU publication?
yes
id
a8db629c-6a72-45c1-ad58-1d94282aaaa8 (old id 259926)
date added to LUP
2007-10-22 17:55:02
date last changed
2017-12-10 03:43:39
@article{a8db629c-6a72-45c1-ad58-1d94282aaaa8,
  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 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.},
  author       = {Favrin, Giorgio and Irbäck, Anders and Mohanty, Sandipan},
  issn         = {1542-0086},
  language     = {eng},
  number       = {6},
  pages        = {3657--3664},
  publisher    = {Cell Press},
  series       = {Biophysical Journal},
  title        = {Oligomerization of amyloid A beta(16-22) peptides using hydrogen bonds and hydrophobicity forces},
  url          = {http://dx.doi.org/10.1529/biophysj.104.046839},
  volume       = {87},
  year         = {2004},
}