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

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Oligomerization of amyloid A beta(16-22) peptides using hydrogen bonds and hydrophobicity forces. / Favrin, Giorgio; Irbäck, Anders; Mohanty, Sandipan.

In: Biophysical Journal, Vol. 87, No. 6, 2004, p. 3657-3664.

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T1 - Oligomerization of amyloid A beta(16-22) peptides using hydrogen bonds and hydrophobicity forces

AU - Favrin, Giorgio

AU - Irbäck, Anders

AU - Mohanty, Sandipan

PY - 2004

Y1 - 2004

N2 - 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.

AB - 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.

U2 - 10.1529/biophysj.104.046839

DO - 10.1529/biophysj.104.046839

M3 - Article

VL - 87

SP - 3657

EP - 3664

JO - Biophysical Journal

JF - Biophysical Journal

SN - 1542-0086

IS - 6

ER -