Nickel(II) complexes of the multihistidine peptide fragments of human prion protein

Ildikó Turi, C. Kállay, Dorina Szikszai, Giuseppe Pappalardo, Giuseppe Di Natale, Paolo De Bona, Enrico Rizzarelli, I. Sóvágó

Research output: Contribution to journalArticle

25 Citations (Scopus)

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).

Original languageEnglish
Pages (from-to)885-891
Number of pages7
JournalJournal of Inorganic Biochemistry
Volume104
Issue number8
DOIs
Publication statusPublished - Aug 2010

Fingerprint

Peptide Fragments
Nickel
Copper
Peptides
Binding Sites
Ions
Deprotonation
Circular Dichroism
Prions
Prion Proteins
Histidine
Amides
Isomers
Nitrogen
Metals
Atoms

Keywords

  • Circular dichroism
  • Histidine
  • Nickel(II)
  • Peptides
  • Prion protein
  • Stability constants

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Nickel(II) complexes of the multihistidine peptide fragments of human prion protein. / Turi, Ildikó; Kállay, C.; Szikszai, Dorina; Pappalardo, Giuseppe; Di Natale, Giuseppe; De Bona, Paolo; Rizzarelli, Enrico; Sóvágó, I.

In: Journal of Inorganic Biochemistry, Vol. 104, No. 8, 08.2010, p. 885-891.

Research output: Contribution to journalArticle

Turi, Ildikó ; Kállay, C. ; Szikszai, Dorina ; Pappalardo, Giuseppe ; Di Natale, Giuseppe ; De Bona, Paolo ; Rizzarelli, Enrico ; Sóvágó, I. / Nickel(II) complexes of the multihistidine peptide fragments of human prion protein. In: Journal of Inorganic Biochemistry. 2010 ; Vol. 104, No. 8. pp. 885-891.
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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).",
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T1 - Nickel(II) complexes of the multihistidine peptide fragments of human prion protein

AU - Turi, Ildikó

AU - Kállay, C.

AU - Szikszai, Dorina

AU - Pappalardo, Giuseppe

AU - Di Natale, Giuseppe

AU - De Bona, Paolo

AU - Rizzarelli, Enrico

AU - Sóvágó, I.

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N2 - 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).

AB - 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).

KW - Circular dichroism

KW - Histidine

KW - Nickel(II)

KW - Peptides

KW - Prion protein

KW - Stability constants

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