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Biochem Biophys Res Commun. 2011 Jul 29;411(2):312-6. doi: 10.1016/j.bbrc.2011.06.133. Epub 2011 Jun 25.

A partially folded structure of amyloid-beta(1-40) in an aqueous environment.

Author information

1
Department of Biophysics, University of Michigan, Ann Arbor, MI 48109-1055, USA.

Abstract

Aggregation of the Aβ(1-40) peptide is linked to the development of extracellular plaques characteristic of Alzheimer's disease. While previous studies commonly show the Aβ(1-40) is largely unstructured in solution, we show that Aβ(1-40) can adopt a compact, partially folded structure. In this structure (PDB ID: 2LFM), the central hydrophobic region of the peptide forms a 3(10) helix from H13 to D23 and the N- and C-termini collapse against the helix due to the clustering of hydrophobic residues. Helical intermediates have been predicted to be crucial on-pathway intermediates in amyloid fibrillogenesis, and the structure presented here presents a new target for investigation of early events in Aβ(1-40) fibrillogenesis.

PMID:
21726530
PMCID:
PMC3148408
DOI:
10.1016/j.bbrc.2011.06.133
[Indexed for MEDLINE]
Free PMC Article

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