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Inorg Chem. 2011 Mar 7;50(5):1614-8. doi: 10.1021/ic100967s. Epub 2011 Jan 31.

Affinity of Cu+ for the copper-binding domain of the amyloid-β peptide of Alzheimer's disease.

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Department of Chemistry & Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland 21250, USA.


The role of metal ions in Alzheimer's disease etiology is unresolved. For the redox-active metal ions iron and copper, the formation of reactive oxygen species by metal amyloid complexes has been proposed to contribute to Alzheimer's disease neurodegeneration. For copper, reactive oxygen species are generated by copper redox cycling between its 1+ and 2+ oxidation states. Thus, the AβCu(I) complex is potentially a critical reactant associated with Alzheimer's disease etiology. Through competitive chelation, we have measured the affinity of the soluble copper-binding domain of the amyloid-β peptide for Cu(I). The dissociation constants are in the femtomolar range for both wild-type and histidine-to-alanine mutants. These results indicate that Cu(I) binds more tightly to monomeric amyloid-β than Cu(II) does, which leads us to propose that Cu(I) is a relevant in vivo oxidation state.

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