The role of histidine residue in coordination abilities of peptides with multi histidine sequence towards nickel(II) ions

A. Matera, J. Brasuń, M. Cebrat, J. Światek-Kozłowska

Research output: Contribution to journalArticle

Abstract

Previous studies on the histidine rich peptides-Cu2+ systems have shown very efficient coordination abilities and high termodynamic stability of the complexes formed. In this work the ability of histidine-rich peptides with Ni2+ ions are presented. The coordination abilities of the series of the N-protected (Ac-His-Arg-His-Gly-His-Gly, Ac-His-Gly-His-Arg-His- Gly, Ac-Gly-His-His-Arg-His-Gly, Ac-His-His-Gly-His-Arg-Gly) and unprotected peptides (His-Arg-His-Gly-His-Gly, His-Gly-His-Arg-His-Gly, Gly-His-His-Arg-His- Gly, and His-His-Gly-His-Arg-Gly) towards Ni2+ ions were studied by spectroscopic (UV/VIS, CD) and potentiometric methods. For the N-protected peptides the dominant complex species with {3Nim} in physiological pH range has been determined, while for the unprotected peptides the coordination of the first amide nitrogen takes place. Moreover, for the Ni 2+-peptide systems the complexes with two geometries were determined: the paramagnetic octahedral species within the acidic pH range and the diamagnetic square-planar species at pH exceeding 7.

Original languageEnglish (US)
Pages (from-to)1367-1382
Number of pages16
JournalPolish Journal of Chemistry
Volume82
Issue number7
StatePublished - Jul 2008
Externally publishedYes

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Nickel
Histidine
Ions
Peptides
Amides
Nitrogen
Geometry

Keywords

  • Complexes
  • Coordination chemistry
  • Histidine
  • Nickel
  • Peptides

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

The role of histidine residue in coordination abilities of peptides with multi histidine sequence towards nickel(II) ions. / Matera, A.; Brasuń, J.; Cebrat, M.; Światek-Kozłowska, J.

In: Polish Journal of Chemistry, Vol. 82, No. 7, 07.2008, p. 1367-1382.

Research output: Contribution to journalArticle

Matera, A, Brasuń, J, Cebrat, M & Światek-Kozłowska, J 2008, 'The role of histidine residue in coordination abilities of peptides with multi histidine sequence towards nickel(II) ions', Polish Journal of Chemistry, vol. 82, no. 7, pp. 1367-1382.
Matera, A. ; Brasuń, J. ; Cebrat, M. ; Światek-Kozłowska, J. / The role of histidine residue in coordination abilities of peptides with multi histidine sequence towards nickel(II) ions. In: Polish Journal of Chemistry. 2008 ; Vol. 82, No. 7. pp. 1367-1382.
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AB - Previous studies on the histidine rich peptides-Cu2+ systems have shown very efficient coordination abilities and high termodynamic stability of the complexes formed. In this work the ability of histidine-rich peptides with Ni2+ ions are presented. The coordination abilities of the series of the N-protected (Ac-His-Arg-His-Gly-His-Gly, Ac-His-Gly-His-Arg-His- Gly, Ac-Gly-His-His-Arg-His-Gly, Ac-His-His-Gly-His-Arg-Gly) and unprotected peptides (His-Arg-His-Gly-His-Gly, His-Gly-His-Arg-His-Gly, Gly-His-His-Arg-His- Gly, and His-His-Gly-His-Arg-Gly) towards Ni2+ ions were studied by spectroscopic (UV/VIS, CD) and potentiometric methods. For the N-protected peptides the dominant complex species with {3Nim} in physiological pH range has been determined, while for the unprotected peptides the coordination of the first amide nitrogen takes place. Moreover, for the Ni 2+-peptide systems the complexes with two geometries were determined: the paramagnetic octahedral species within the acidic pH range and the diamagnetic square-planar species at pH exceeding 7.

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