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J Phys Chem B. 2008 Aug 14;112(32):9998-10004. doi: 10.1021/jp801222x. Epub 2008 Jul 23.

Characterizing the first steps of amyloid formation for the ccbeta peptide.

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1
University Chemical Laboratories, Lensfield Road, Cambridge CB2 1EW, United Kingdom.

Abstract

We employ constant-temperature and replica exchange molecular dynamics to survey the free energy landscape of the ccbeta peptide using a united-atom potential and an implicit solvent representation. Starting from the experimental coiled-coil structure we observe alpha to beta conversion on increasing the temperature, in agreement with experiment. Various beta-sheet trimers are identified as free energy minima, including one that closely resembles the amyloid beta-sheet model previously proposed from experimental data. We characterize two alternative pathways leading to beta-sheets. The first proceeds via direct alpha to beta conversion without dissociation of the trimer, and the second can be classified as a dissociation/reassociation pathway.

PMID:
18646795
DOI:
10.1021/jp801222x
[Indexed for MEDLINE]

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