Heteronuclear and homonuclear Cu2+ and Zn2+ complexes with multihistidine peptides based on zebrafish prion-like protein.
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.
Valensin
Daniela
D
Department of Chemistry, University of Siena, Via Aldo Moro, 53100 Siena, Italy. valensindan@unisi.it
Szyrwiel
Łukasz
Ł
Camponeschi
Francesca
F
Rowińska-Zyrek
Magdalena
M
Molteni
Elena
E
Jankowska
Elzbieta
E
Szymanska
Aneta
A
Gaggelli
Elena
E
Valensin
Gianni
G
Kozłowski
Henryk
H
D000818:Animals; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D006639:Histidine / Q000737:chemistry / Q000378:metabolism; D007536:Isomerism; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011328:Prions / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D015027:Zebrafish / Q000378:metabolism*; D015032:Zinc / Q000737:chemistry* / Q000378:metabolism
D010455:Peptides; D011328:Prions; D006639:Histidine; D003300:Copper; D015032:Zinc