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Selective destabilization of soluble amyloid beta oligomers by divalent metal ions.

Abstract：

:Aggregation of the amyloid beta (Abeta) peptide yields both fibrillar precipitates and soluble oligomers, and is associated with Alzheimer's disease (AD). In vitro, Cu(2+) and Zn(2+) strongly bind Abeta and promote its precipitation. However, less is known about their interactions with the soluble oligomers, which are thought to be the major toxic species responsible for AD. Using fluorescence correlation spectroscopy to resolve the various soluble species of Abeta, we show that low concentrations of Cu(2+) (1 microM) and Zn(2+) (4 microM) selectively eliminate the oligomeric population (within approximately 2h), while Mg(2+) displays a similar effect at a higher concentration (60 microM). This uncovers a new aspect of Abeta-metal ion interactions, as precipitation is not substantially altered at these low metal ion concentrations. Our results suggest that physiological concentrations of Cu(2+) and Zn(2+) can critically alter the stability of the toxic Abeta oligomers and can potentially control the course of neurodegeneration.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Garai K,Sengupta P,Sahoo B,Maiti S

doi

10.1016/j.bbrc.2006.04.056

subject

Has Abstract

pub_date

2006-06-23 00:00:00

pages

210-5

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)00878-3

journal_volume

345

pub_type

杂志文章

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