The effect of non-coordinating side chains on the metal binding affinities of peptides of histidine

Ildikó Turi, Daniele Sanna, Eugenio Garribba, Giuseppe Pappalardo, I. Sóvágó

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Copper(II), nickel(II) and zinc(II) complexes of both N-terminally acetylated and free tetrapeptides modeling the sequences at H96 (GTHS) and H111 (MKHM) sites of prion protein have been studied by potentiometric and various spectroscopic (UV-Vis, CD, EPR and NMR) techniques. Complex formation processes of the two tetrapeptides are very similar but copper(II) ions have enhanced affinity to form complexes with the - MKHM-sequence, while the opposite trend was obtained for nickel(II). The selectivity of metal binding of peptides was supported by DFT calculations, too. Three octapeptides NH2-GTHSMKHM- NH2, NH2-MKHMGTHS-NH2 and Ac-GTHSMKHM-NH 2 containing the previous tetrapeptide domains have also been synthesized and studied with the same metal ions. All octapeptides are able to bind two copper(II) or nickel(II) ions and the histidyl residues are the primary metal binding sites. In the case of the N-terminally free octapeptides the first metal ion is always bonded to the amino terminus of both peptides reflecting the outstanding thermodynamic stability of the albumin-like binding site. The presence of coordination isomers was, however, identified for the mononuclear species of Ac-GTHSMKHM-NH2 with a preference for copper(II) and nickel(II) binding at MKHM and GTHS sites, respectively. These data suggest that the specific sequences of prion fragments are responsible for the metal ion selectivity. Mixed metal copper(II)-nickel(II) complexes are also formed with all peptides showing the same preferences for metal binding as it was obtained for the binary systems.

Original languageEnglish
Pages (from-to)7-17
Number of pages11
JournalPolyhedron
Volume62
DOIs
Publication statusPublished - 2013

Fingerprint

histidine
Nickel
Histidine
Peptides
peptides
affinity
Copper
Metals
nickel
copper
Metal ions
metal ions
metals
Binding sites
selectivity
Binding Sites
Ions
Prions
albumins
Discrete Fourier transforms

Keywords

  • Copper(II)
  • Histidine
  • Nickel(II)
  • Peptides
  • Stability constants
  • Zinc(II)

ASJC Scopus subject areas

  • Inorganic Chemistry
  • Materials Chemistry
  • Physical and Theoretical Chemistry

Cite this

The effect of non-coordinating side chains on the metal binding affinities of peptides of histidine. / Turi, Ildikó; Sanna, Daniele; Garribba, Eugenio; Pappalardo, Giuseppe; Sóvágó, I.

In: Polyhedron, Vol. 62, 2013, p. 7-17.

Research output: Contribution to journalArticle

Turi, Ildikó ; Sanna, Daniele ; Garribba, Eugenio ; Pappalardo, Giuseppe ; Sóvágó, I. / The effect of non-coordinating side chains on the metal binding affinities of peptides of histidine. In: Polyhedron. 2013 ; Vol. 62. pp. 7-17.
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N2 - Copper(II), nickel(II) and zinc(II) complexes of both N-terminally acetylated and free tetrapeptides modeling the sequences at H96 (GTHS) and H111 (MKHM) sites of prion protein have been studied by potentiometric and various spectroscopic (UV-Vis, CD, EPR and NMR) techniques. Complex formation processes of the two tetrapeptides are very similar but copper(II) ions have enhanced affinity to form complexes with the - MKHM-sequence, while the opposite trend was obtained for nickel(II). The selectivity of metal binding of peptides was supported by DFT calculations, too. Three octapeptides NH2-GTHSMKHM- NH2, NH2-MKHMGTHS-NH2 and Ac-GTHSMKHM-NH 2 containing the previous tetrapeptide domains have also been synthesized and studied with the same metal ions. All octapeptides are able to bind two copper(II) or nickel(II) ions and the histidyl residues are the primary metal binding sites. In the case of the N-terminally free octapeptides the first metal ion is always bonded to the amino terminus of both peptides reflecting the outstanding thermodynamic stability of the albumin-like binding site. The presence of coordination isomers was, however, identified for the mononuclear species of Ac-GTHSMKHM-NH2 with a preference for copper(II) and nickel(II) binding at MKHM and GTHS sites, respectively. These data suggest that the specific sequences of prion fragments are responsible for the metal ion selectivity. Mixed metal copper(II)-nickel(II) complexes are also formed with all peptides showing the same preferences for metal binding as it was obtained for the binary systems.

AB - Copper(II), nickel(II) and zinc(II) complexes of both N-terminally acetylated and free tetrapeptides modeling the sequences at H96 (GTHS) and H111 (MKHM) sites of prion protein have been studied by potentiometric and various spectroscopic (UV-Vis, CD, EPR and NMR) techniques. Complex formation processes of the two tetrapeptides are very similar but copper(II) ions have enhanced affinity to form complexes with the - MKHM-sequence, while the opposite trend was obtained for nickel(II). The selectivity of metal binding of peptides was supported by DFT calculations, too. Three octapeptides NH2-GTHSMKHM- NH2, NH2-MKHMGTHS-NH2 and Ac-GTHSMKHM-NH 2 containing the previous tetrapeptide domains have also been synthesized and studied with the same metal ions. All octapeptides are able to bind two copper(II) or nickel(II) ions and the histidyl residues are the primary metal binding sites. In the case of the N-terminally free octapeptides the first metal ion is always bonded to the amino terminus of both peptides reflecting the outstanding thermodynamic stability of the albumin-like binding site. The presence of coordination isomers was, however, identified for the mononuclear species of Ac-GTHSMKHM-NH2 with a preference for copper(II) and nickel(II) binding at MKHM and GTHS sites, respectively. These data suggest that the specific sequences of prion fragments are responsible for the metal ion selectivity. Mixed metal copper(II)-nickel(II) complexes are also formed with all peptides showing the same preferences for metal binding as it was obtained for the binary systems.

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