Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5657
Title: Heteronuclear and homonuclear Cu2+ and Zn2+ complexes with multihistidine peptides based on zebrafish prion-like protein
Authors: Valensin, Daniela 
Szyrwiel, L.
Camponeschi, Francesca
ROWINSKA ZYREK, M
Molteni, E
Jankowska, E
Szymanska, A
Gaggelli, Elena 
Valensin, Gianni 
Kozlowski, H.
Issue Date: 2009
Project: None 
Journal: INORGANIC CHEMISTRY
Abstract: 
The homeostasis of metal ions, especially copper and zinc, is a major factor that may influence the prion diseases and the biological function of prion protein (PrP). The His-rich regions are basic sites for metal binding and antioxidant activity of the PrP structures. Animal prion-like proteins contain also His-rich domains, and their coordination chemistry may provide better insight into the chemistry and biology of PrP structures and related diseases. Herein, we report an equilibrium study on heteronuclear Zn2+-Cu2+ complexes with zrel-PrP fragments from zebrafish. Potentiometric, spectroscopic, and mass spectrometric methods showed that the binding of copper is much more effective than the binding of zinc. At physiological pH, both metals bind to the histidine imidazole N donors of the studied peptides.
Description: 
35714
URI: http://hdl.handle.net/20.500.12779/5657
ISSN: 0020-1669
DOI: 10.1021/ic9008202
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