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Issue 2, 2012
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Zn induced structural aggregation patterns of β-amyloid peptides by first-principle simulations and XAS measurements

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Abstract

We show in this paper that in the presence of Zn ions a peculiar structural aggregation pattern of β-amyloid peptides in which metal ions are sequentially coordinated to either three or four histidines of nearby peptides is favored. To stabilize this configuration a deprotonated imidazole ring from one of the histidines forms a bridge connecting two adjacent Zn ions. Though present in zeolite imidazolate frameworks, remarkably in biological compounds this peculiar Zn–imidazolate–Zn topology is only found in enzymes belonging to the Cu,Zn-superoxide dismutase family in the form of an imidazolate bridging Cu and Zn. The results we present are obtained by combining X-ray absorption spectroscopy experimental data with detailed first-principle molecular dynamics simulations.

Graphical abstract: Zn induced structural aggregation patterns of β-amyloid peptides by first-principle simulations and XAS measurements

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Publication details

The article was received on 01 Sep 2011, accepted on 25 Nov 2011 and first published on 15 Dec 2011


Article type: Paper
DOI: 10.1039/C2MT00148A
Citation: Metallomics, 2012,4, 156-165
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    Zn induced structural aggregation patterns of β-amyloid peptides by first-principle simulations and XAS measurements

    P. Giannozzi, K. Jansen, G. L. Penna, V. Minicozzi, S. Morante, G. Rossi and F. Stellato, Metallomics, 2012, 4, 156
    DOI: 10.1039/C2MT00148A

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