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:
https://lup.lub.lu.se/record/259926
- author
- Favrin, Giorgio
LU
; Irbäck, Anders
LU
and Mohanty, Sandipan
LU
- organization
- publishing date
- 2004
- 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
- 2016-04-01 11:52:04
- date last changed
- 2025-10-14 12:32:50
@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}},
doi = {{10.1529/biophysj.104.046839}},
volume = {{87}},
year = {{2004}},
}