Zn2+'s ability to alter the distribution of Cu2+ among the available binding sites of A beta(1-16)-polyethylenglycol-ylated peptide: Implications in Alzheimer's disease
Zn2+'s ability to alter the distribution of Cu2+ among the available binding sites of A beta(1-16)-polyethylenglycol-ylated peptide: Implications in Alzheimer's disease(696 views) Damante CA, Ösz K, Nagy Z, Grasso G, Pappalardo G, Rizzarelli E, Sóvágó I
Department of Chemical Sciences, University of Catania, V.le A. Doria 6, 95125 Catania, Italy
Department of Physical Chemistry, University of Debrecen, 4010 Debrecen, Hungary
Department of Inorganic and Analytical Chemistry, University of Debrecen, 4010 Debrecen, Hungary
CNR Institute of Biostructures and Bioimaging, V.le A. Doria 6, 95125 Catania, Italy
References: Not available.
Zn2+'s ability to alter the distribution of Cu2+ among the available binding sites of A beta(1-16)-polyethylenglycol-ylated peptide: Implications in Alzheimer's disease
The formation of mixed copper (II) and zinc (II) complexes with Abeta (1-16) -PEG has been investigated. The peptide fragment forms stable mixed metal complexes at physiological pH in which the His13/His14 dyad is the zinc (II) 's preferred binding site, while copper (II) coordination occurs at the N-terminus also involving the His6 imidazole. Copper (II) is prevented by zinc (II) excess from the binding to the two His residues, His13 and His14. As the latter binding mode has been recently invoked to explain the redox activity of the copper-Abeta complex, the formation of ternary metal complexes may justify the recently proposed protective role of zinc (II) in Alzheimer's disease. Therefore, the reported results suggest that zinc (II) competes with copper for Abeta binding and inhibits copper-mediated Abeta redox chemistry. 2011 American Chemical Society
Zn2+'s ability to alter the distribution of Cu2+ among the available binding sites of A beta(1-16)-polyethylenglycol-ylated peptide: Implications in Alzheimer's disease
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Zn2+'s ability to alter the distribution of Cu2+ among the available binding sites of A beta(1-16)-polyethylenglycol-ylated peptide: Implications in Alzheimer's disease
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(517 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote