Back to Search
Start Over
Heteronuclear and homonuclear Cu2+ and Zn2+ complexes with multihistidine peptides based on zebrafish prion-like protein.
- Source :
-
Inorganic chemistry [Inorg Chem] 2009 Aug 03; Vol. 48 (15), pp. 7330-40. - Publication Year :
- 2009
-
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.
- Subjects :
- Animals
Circular Dichroism
Copper metabolism
Histidine chemistry
Histidine metabolism
Isomerism
Nuclear Magnetic Resonance, Biomolecular
Peptides metabolism
Prions metabolism
Protein Binding
Zinc metabolism
Copper chemistry
Peptides chemistry
Prions chemistry
Zebrafish metabolism
Zinc chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1520-510X
- Volume :
- 48
- Issue :
- 15
- Database :
- MEDLINE
- Journal :
- Inorganic chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 19586023
- Full Text :
- https://doi.org/10.1021/ic9008202