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Intrinsic thermal expansivity and hydrational properties of amyloid peptide Abeta42 in liquid water
Volumetric and conformational properties of the amyloid (1–42) peptide (A42) are studied in relation to the properties of hydration water in a wide temperature range by computer simulations. The...

The Alzheimer beta-amyloid (Abeta1–39) dimer in an implicit solvent

J. Chem. Phys. 129, 195102 (2008); doi:10.1063/1.3021062

Published 21 November 2008

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Priya Anand,1 Fateh S. Nandel,1 and Ulrich H. E. Hansmann2
1Department of Biophysics, Panjab University, Chandigarh-160014, India
2Department of Physics, Michigan Technological University, Houghton, Michigan 49931, USA
Oligomers of Abeta peptides are suspected as the underlying cause of Alzheimer disease. Knowledge of their structural properties could therefore lead to a deeper understanding of the mechanism behind the outbreak of this disease. As a step in this direction we have studied Abeta dimers by all-atom molecular dynamics simulations. Equilibrated structures at 300 K were clustered into different families with similar structural features. The dominant cluster has parallel N-terminals and a well defined segment Leu17-Ala21 that are stabilized by salt bridges between Lys28 of one chain and either Glu22 or Asp23 of the other chain. The formation of these salt bridges may be the limiting step in oligomerization and fibrillogenesis. ©2008 American Institute of Physics
History: Received 15 September 2008; accepted 14 October 2008; published 21 November 2008
Permalink: http://link.aip.org/link/?JCPSA6/129/195102/1
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