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 language | English |
|---|---|
| Pages (from-to) | 1399-1409 |
| Number of pages | 11 |
| Journal | Journal of Inorganic Biochemistry |
| Volume | 100 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - Aug 2006 |
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Keywords
- Histidine
- Imidazole
- Prion protein
- Transition metal ions
ASJC Scopus subject areas
- Biochemistry
- Inorganic Chemistry
Cite this
Transition metal complexes of terminally protected peptides containing histidyl residues. / Jószai, Viktória; Nagy, Zoltán; Ősz, K.; Sanna, Daniele; Di Natale, Giuseppe; La Mendola, Diego; Pappalardo, Giuseppe; Rizzarelli, Enrico; Sóvágó, I.
In: Journal of Inorganic Biochemistry, Vol. 100, No. 8, 08.2006, p. 1399-1409.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Transition metal complexes of terminally protected peptides containing histidyl residues
AU - Jószai, Viktória
AU - Nagy, Zoltán
AU - Ősz, K.
AU - Sanna, Daniele
AU - Di Natale, Giuseppe
AU - La Mendola, Diego
AU - Pappalardo, Giuseppe
AU - Rizzarelli, Enrico
AU - Sóvágó, I.
PY - 2006/8
Y1 - 2006/8
N2 - 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.
AB - 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.
KW - Histidine
KW - Imidazole
KW - Prion protein
KW - Transition metal ions
UR - http://www.scopus.com/inward/record.url?scp=33745727006&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33745727006&partnerID=8YFLogxK
U2 - 10.1016/j.jinorgbio.2006.04.003
DO - 10.1016/j.jinorgbio.2006.04.003
M3 - Article
C2 - 16730799
AN - SCOPUS:33745727006
VL - 100
SP - 1399
EP - 1409
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
SN - 0162-0134
IS - 8
ER -