Research article summary (published 29 Sep 2009):

Interpeptide interactions induce helix to strand structural transition in Abeta peptides.

Full Abstract

Replica exchange molecular dynamics and all-atom implicit solvent model are used to compute the structural propensities in Abeta monomers, dimers, and Abeta peptides bound to the edge of amyloid fibril. These systems represent, on an approximate level, different stages in Abeta aggregation. Abeta monomers are shown to form helical structure in the N-terminal (residues 13 to 21). Interpeptide interactions in Abeta dimers and, especially, in the peptides bound to the fibril induce a dramatic shift in the secondary structure, from helical states toward beta-strand conformations. The sequence region 10-23 in Abeta peptide is found to form most of interpeptide interactions upon aggregation. Simulation results are tested by comparing the chemical shifts in Abeta monomers computed from simulations and obtained experimentally. Possible implications of our simulations for designing aggregation-resistant variants of Abeta are discussed.

Author information

Author/s: Takeda, Takako (T); Klimov, Dmitri K (DK);

Affiliation: Department of Bioinformatics and Computational Biology, George Mason University, Manassas, Virginia 20110, USA.

Grants: R01 AG028191 (Agency:NIA NIH HHS)

Journal and publication information

Publication Type: Journal Article; Research Support, N.I.H., Extramural

Journal: Proteins (Proteins), published in United States. (Language: eng)

Reference: 2009-Oct; vol 77 (issue 1) : pp 1-13

Dates: Created 2009/08/24; Completed 2009/10/29;

PMID: 19350616, status: MEDLINE (last retrieval date: 10/29/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Amyloid beta-Protein - chemistry Animals Computer Simulation Humans Models, Molecular

Models, Molecular Peptide Fragments - chemistry Protein Binding Protein Multimerization Protein Structure, Secondary

Associated Chemicals: Amyloid beta-Protein (0) ; Peptide Fragments (0)

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