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Heteronuclear and Homonuclear Cu 2+ and Zn 2+ Complexes with Multihistidine Peptides Based on Zebrafish Prion-like Protein

2009; American Chemical Society; Volume: 48; Issue: 15 Linguagem: Inglês

10.1021/ic9008202

1520-510X

Daniela Valensin, Łukasz Szyrwiel, Francesca Camponeschi, Magdalena Rowińska‐Żyrek, Elena Molteni, Elżbieta Jankowska, Aneta Szymańska, Elena Gaggelli, Gianni Valensin, Henryk Kozłowski,

Crystallography and molecular interactions

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.