Transition metal complexes of terminally protected peptides containing histidyl residues

Viktória Jószai, Zoltán Nagy, Katalin Osz, Daniele Sanna, Giuseppe Di Natale, Diego La Mendola, Giuseppe Pappalardo, Enrico Rizzarelli, Imre Sóvágó

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Abstract

Histidine-containing peptide fragments of prion protein are efficient ligands to bind various transition metal ions and they have high selectivity in metal binding. The metal ion affinity follows the order: Pd(II) ≫ Cu(II) ≫ Ni(II) ≥ Zn(II) > Cd(II) ∼ Co(II) > Mn(II). The high selectivity of metal binding is connected to the involvement of both imidazole and amide nitrogen atoms in metal binding for Pd(II), Cu(II) and Ni(II), while only the monodentate Nim-coordination is possible with the other metal ions. The stoichiometry and binding mode of palladium(II) complexes show great variety depending on the metal ion to ligand ratio, pH and especially the presence of coordinating donor atoms in the side chains of peptide fragments. It is also clear from our data that the peptide fragments containing histidine outside the octarepeat (His96, His111 and His187) are more efficient ligands than the monomer peptide fragments of the octarepeat domain.

Original languageEnglish
Pages (from-to)1399-1409
Number of pages11
JournalJournal of Inorganic Biochemistry
Volume100
Issue number8
DOIs
Publication statusPublished - Aug 1 2006

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Keywords

  • Histidine
  • Imidazole
  • Prion protein
  • Transition metal ions

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

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