http://www.cnr.it/ontology/cnr/individuo/prodotto/ID14234
Nickel(II) complexes of the multihistidine peptide fragments of human prion protein (Articolo in rivista)
- Type
- Label
- Nickel(II) complexes of the multihistidine peptide fragments of human prion protein (Articolo in rivista) (literal)
- Anno
- 2010-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.jinorgbio.2010.04.008 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- I. Turi1; C. Kállay1; D. Szikszai1; G. Pappalardo2; G. Di Natale3; P. De Bona3; E. Rizzarelli3; I. Sóvágó1. (literal)
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- Rivista
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1 University of Debrecen, Department of Inorganic and Analytical Chemistry, H-4010 Debrecen, Hungary
2 CNR, Institute of Biostructures and Bioimaging, Catania 95125 Catania, Italy
3 University of Catania, Department of Chemical Sciences, 95125 Catania, Italy (literal)
- Titolo
- Nickel(II) complexes of the multihistidine peptide fragments of human prion protein (literal)
- Abstract
- Nickel(II) complexes of the peptide fragments of human prion protein containing histidyl residues both inside
and outside the octarepeat domain have been studied by the combined application of potentiometric, UV-
visible and circular dichroism spectroscopic methods. The imidazole-N donor atoms of histidyl residues are the
exclusive metal binding sites below pH 7.5, but the formation of stable macrochelates was characteristic only
for the peptide HuPrP(76-114) containing four histidyl residues. Yellow colored square planar complexes
were obtained above pH 7.5-8 with the cooperative deprotonation of three amide nitrogens in the [Nim,N-,N-,
N-] coordination mode. It was found that the peptides can bind as many nickel(II) ions as the number of
independent histidyl residues. All data supported that the complex formation processes of nickel(II) are very
similar to those of copper(II), but with a significantly reduced stability for nickel(II), which shifts the complex
formation reactions into the slightly alkaline pH range. The formation of coordination isomers was
characteristic of the mononuclear complexes with a significant preference for the nickel(II) binding at the
histidyl sites outside the octarepeat domain. The results obtained for the two-histidine fragments of the
protein, HuPrP(91-115), HuPrP(76-114)H85A and HuPrP(84-114)H96A, made it possible to compare the
binding ability of the His96 and His111 sites. These data reveal a significant difference in the nickel(II) and
copper(II) binding sites of the peptides: His96 was found to predominate almost completely for nickel(II) ions,
while the opposite order, but with comparable concentrations, was reported for copper(II). (literal)
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