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001-es BibID:BIBFORM016490
Első szerző:Turi Ildikó (vegyész)
Cím:Nickel(II) complexes of the multihistidine peptide fragments of human prion protein / Ildikó Turi, Csilla Kállay, Dorina Szikszai, Giuseppe Pappalardo, Giuseppe Di Natale, Paolo De Bona, Enrico Rizzarelli, Imre Sóvágó
Dátum:2010
ISSN:0162-0134
Megjegyzések: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 [N-im,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). (C) 2010 Elsevier Inc. All rights reserved.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Prion protein
Peptides
Nickel(II)
Stability constants
Histidine
Circular dichroism
unstructured amyloidogenic region
copper-binding
octarepeat domain
histidyl residues
circular-dichroism
coordination modes
cu2+
coordination
stability
constants
sites
Megjelenés:Journal of Inorganic Biochemistry. - 104 : 8 (2010), p. 885-891. -
További szerzők:Kállay Csilla (1978-) (vegyész) Szikszai Dorina (1985-) (vegyész) Pappalardo, Giuseppe Di Natale, Giuseppe De Bona, Paolo Rizzarelli, Enrico Sóvágó Imre (1946-) (vegyész)
Internet cím:DOI
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