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

Research output: Contribution to journalArticle

Bibtex

@article{a8db629c6a7245c1ad581d94282aaaa8,
title = "Oligomerization of amyloid A beta(16-22) peptides using hydrogen bonds and hydrophobicity forces",
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 = "Giorgio Favrin and Anders Irb{\"a}ck and Sandipan Mohanty",
year = "2004",
doi = "10.1529/biophysj.104.046839",
language = "English",
volume = "87",
pages = "3657--3664",
journal = "Biophysical Journal",
issn = "1542-0086",
publisher = "Cell Press",
number = "6",

}