Thermodynamic and structural characterization of the copper(II) complexes of peptides containing both histidyl and aspartyl residues

Csilla Kállay, Zoltán Nagy, Katalin Várnagy, Gerasimos Malandrinos, Nick Hadjiliadis, Imre Sóvágó

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Abstract

Terminally protected pentapeptides with 2 histidines (Ac-HHVGD- NH2 and Ac-HVGDH- NH2) and the terminally free peptides containing both internal aspartyl and C-terminal histidyl residues (FDAH and VIDAH) have been synthesized, and copper(II) complexes studied by potentiometric, UV-Vis, CD, and EPR spectroscopic techniques in solution. Both thermodynamic and spectroscopic data reveal that side chain donor atoms of aspartyl and histidyl residues have a significant contribution to the metal binding affinity of peptide molecules. In the case of terminally protected peptides, the role of the imidazole-N donor functions is reflected in the enhanced stability of the 3N and 4N coordinated copper(II) complexes. The amino and β-carboxylate groups of FDAH and VIDAH create a very effective metal binding site with the ( NH 2, N-, β- COO -) and ( NH 2, N-, N-, β- COO -) coordination modes including the N-termini, while the histidine sites are available for the formation of the ( N im, N-, N-) binding mode resulting in the preference of dinuclear complex formation.

Original languageEnglish
Article number30394
JournalBioinorganic Chemistry and Applications
Volume2007
DOIs
Publication statusPublished - 2007

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Thermodynamics
Copper
Histidine
Peptides
Metals
Paramagnetic resonance
Binding Sites
Atoms
Molecules
carboxyl radical

ASJC Scopus subject areas

  • Inorganic Chemistry
  • Organic Chemistry
  • Biochemistry

Cite this

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title = "Thermodynamic and structural characterization of the copper(II) complexes of peptides containing both histidyl and aspartyl residues",
abstract = "Terminally protected pentapeptides with 2 histidines (Ac-HHVGD- NH2 and Ac-HVGDH- NH2) and the terminally free peptides containing both internal aspartyl and C-terminal histidyl residues (FDAH and VIDAH) have been synthesized, and copper(II) complexes studied by potentiometric, UV-Vis, CD, and EPR spectroscopic techniques in solution. Both thermodynamic and spectroscopic data reveal that side chain donor atoms of aspartyl and histidyl residues have a significant contribution to the metal binding affinity of peptide molecules. In the case of terminally protected peptides, the role of the imidazole-N donor functions is reflected in the enhanced stability of the 3N and 4N coordinated copper(II) complexes. The amino and β-carboxylate groups of FDAH and VIDAH create a very effective metal binding site with the ( NH 2, N-, β- COO -) and ( NH 2, N-, N-, β- COO -) coordination modes including the N-termini, while the histidine sites are available for the formation of the ( N im, N-, N-) binding mode resulting in the preference of dinuclear complex formation.",
author = "Csilla K{\'a}llay and Zolt{\'a}n Nagy and Katalin V{\'a}rnagy and Gerasimos Malandrinos and Nick Hadjiliadis and Imre S{\'o}v{\'a}g{\'o}",
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TY - JOUR

T1 - Thermodynamic and structural characterization of the copper(II) complexes of peptides containing both histidyl and aspartyl residues

AU - Kállay, Csilla

AU - Nagy, Zoltán

AU - Várnagy, Katalin

AU - Malandrinos, Gerasimos

AU - Hadjiliadis, Nick

AU - Sóvágó, Imre

PY - 2007

Y1 - 2007

N2 - Terminally protected pentapeptides with 2 histidines (Ac-HHVGD- NH2 and Ac-HVGDH- NH2) and the terminally free peptides containing both internal aspartyl and C-terminal histidyl residues (FDAH and VIDAH) have been synthesized, and copper(II) complexes studied by potentiometric, UV-Vis, CD, and EPR spectroscopic techniques in solution. Both thermodynamic and spectroscopic data reveal that side chain donor atoms of aspartyl and histidyl residues have a significant contribution to the metal binding affinity of peptide molecules. In the case of terminally protected peptides, the role of the imidazole-N donor functions is reflected in the enhanced stability of the 3N and 4N coordinated copper(II) complexes. The amino and β-carboxylate groups of FDAH and VIDAH create a very effective metal binding site with the ( NH 2, N-, β- COO -) and ( NH 2, N-, N-, β- COO -) coordination modes including the N-termini, while the histidine sites are available for the formation of the ( N im, N-, N-) binding mode resulting in the preference of dinuclear complex formation.

AB - Terminally protected pentapeptides with 2 histidines (Ac-HHVGD- NH2 and Ac-HVGDH- NH2) and the terminally free peptides containing both internal aspartyl and C-terminal histidyl residues (FDAH and VIDAH) have been synthesized, and copper(II) complexes studied by potentiometric, UV-Vis, CD, and EPR spectroscopic techniques in solution. Both thermodynamic and spectroscopic data reveal that side chain donor atoms of aspartyl and histidyl residues have a significant contribution to the metal binding affinity of peptide molecules. In the case of terminally protected peptides, the role of the imidazole-N donor functions is reflected in the enhanced stability of the 3N and 4N coordinated copper(II) complexes. The amino and β-carboxylate groups of FDAH and VIDAH create a very effective metal binding site with the ( NH 2, N-, β- COO -) and ( NH 2, N-, N-, β- COO -) coordination modes including the N-termini, while the histidine sites are available for the formation of the ( N im, N-, N-) binding mode resulting in the preference of dinuclear complex formation.

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