Metal complexes of peptides containing monodentate or chelating imidazole nitrogen donors

Factors influencing the coordination of amide groups and imidazole side chains

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32 Citations (Scopus)

Abstract

Transition metal complexes of peptides containing monodentate or chelating imidazole side chains have been studied by the combined application of potentiometric and spectroscopic techniques. The results obtained on the complexes of peptides containing C-terminal histidyl residues (Gly3His, Gly4His and Gly5His) provided clear evidence that both amino and imidazole functions are effective metal binding sites. The formation of various macrochelates were described via the coordination of both termini, but the major species were characterised by 4N-coordination starting from the N-termini. The coordination chemistry of a series of peptide molecules containing bis(imidazolyl) agents revealed that the donor functions of the peptide backbone cannot compete with chelation of the bis(imidazolyl) residue. However, the presence of terminal amino group promotes amide coordination, while imidazole residues act as additional donor sites or bridging ligands.

Original languageEnglish
Pages (from-to)149-178
Number of pages30
JournalComments on Inorganic Chemistry
Volume23
Issue number2
DOIs
Publication statusPublished - Mar 2002

Fingerprint

Coordination Complexes
Chelation
Amides
Nitrogen
Peptides
Transition metals
Metals
Binding Sites
Ligands
Molecules
imidazole

Keywords

  • Amide group
  • Bis(imidazolyl) agents
  • Copper(II)
  • Histidyl residues
  • Nickel(II) and zinc(II) complexes
  • Peptides

ASJC Scopus subject areas

  • Inorganic Chemistry

Cite this

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title = "Metal complexes of peptides containing monodentate or chelating imidazole nitrogen donors: Factors influencing the coordination of amide groups and imidazole side chains",
abstract = "Transition metal complexes of peptides containing monodentate or chelating imidazole side chains have been studied by the combined application of potentiometric and spectroscopic techniques. The results obtained on the complexes of peptides containing C-terminal histidyl residues (Gly3His, Gly4His and Gly5His) provided clear evidence that both amino and imidazole functions are effective metal binding sites. The formation of various macrochelates were described via the coordination of both termini, but the major species were characterised by 4N-coordination starting from the N-termini. The coordination chemistry of a series of peptide molecules containing bis(imidazolyl) agents revealed that the donor functions of the peptide backbone cannot compete with chelation of the bis(imidazolyl) residue. However, the presence of terminal amino group promotes amide coordination, while imidazole residues act as additional donor sites or bridging ligands.",
keywords = "Amide group, Bis(imidazolyl) agents, Copper(II), Histidyl residues, Nickel(II) and zinc(II) complexes, Peptides",
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T1 - Metal complexes of peptides containing monodentate or chelating imidazole nitrogen donors

T2 - Factors influencing the coordination of amide groups and imidazole side chains

AU - Sóvágó, I.

AU - Várnagy, K.

AU - Ősz, K.

PY - 2002/3

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N2 - Transition metal complexes of peptides containing monodentate or chelating imidazole side chains have been studied by the combined application of potentiometric and spectroscopic techniques. The results obtained on the complexes of peptides containing C-terminal histidyl residues (Gly3His, Gly4His and Gly5His) provided clear evidence that both amino and imidazole functions are effective metal binding sites. The formation of various macrochelates were described via the coordination of both termini, but the major species were characterised by 4N-coordination starting from the N-termini. The coordination chemistry of a series of peptide molecules containing bis(imidazolyl) agents revealed that the donor functions of the peptide backbone cannot compete with chelation of the bis(imidazolyl) residue. However, the presence of terminal amino group promotes amide coordination, while imidazole residues act as additional donor sites or bridging ligands.

AB - Transition metal complexes of peptides containing monodentate or chelating imidazole side chains have been studied by the combined application of potentiometric and spectroscopic techniques. The results obtained on the complexes of peptides containing C-terminal histidyl residues (Gly3His, Gly4His and Gly5His) provided clear evidence that both amino and imidazole functions are effective metal binding sites. The formation of various macrochelates were described via the coordination of both termini, but the major species were characterised by 4N-coordination starting from the N-termini. The coordination chemistry of a series of peptide molecules containing bis(imidazolyl) agents revealed that the donor functions of the peptide backbone cannot compete with chelation of the bis(imidazolyl) residue. However, the presence of terminal amino group promotes amide coordination, while imidazole residues act as additional donor sites or bridging ligands.

KW - Amide group

KW - Bis(imidazolyl) agents

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KW - Histidyl residues

KW - Nickel(II) and zinc(II) complexes

KW - Peptides

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