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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Vivekanandan S,Brender JR,Lee SY,Ramamoorthy A

doi

10.1016/j.bbrc.2011.06.133

subject

Has Abstract

pub_date

2011-07-29 00:00:00

pages

312-6

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)01114-4

journal_volume

411

pub_type

杂志文章

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