Heteronuclear and homonuclear Cu2+ and Zn2+ complexes with multihistidine peptides based on zebrafish prion-like protein.

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 Zn(2+)-Cu(2+) 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.

DOI: 10.1021/ic9008202

Cite this paper

@article{Valensin2009HeteronuclearAH, title={Heteronuclear and homonuclear Cu2+ and Zn2+ complexes with multihistidine peptides based on zebrafish prion-like protein.}, author={Daniela Valensin and Łukasz Szyrwiel and Francesca Camponeschi and Magdalena Rowińska-Żyrek and Elena Molteni and Elżbieta Jankowska and Aneta Szymańska and Elena Gaggelli and Gianni Valensin and Henryk Kozłowski}, journal={Inorganic chemistry}, year={2009}, volume={48 15}, pages={7330-40} }