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Nickel(ii) and mixed metal complexes of amyloid-β N-terminus
Ist Teil von
Dalton transactions : an international journal of inorganic chemistry, 2010-08, Vol.39 (3), p.746-753
Ort / Verlag
England
Erscheinungsjahr
2010
Quelle
MEDLINE
Beschreibungen/Notizen
Nickel(
ii
) complexes of Aβ(1-16)Y10A and its smaller fragments including Aβ(1-4), Aβ(1-6), Ac-Aβ(1-6) and Ac-Aβ(8-16)Y10A have been studied by potentiometric, UV-Vis and circular dichroism spectroscopic measurements. The formation of mixed metal complexes and the distribution of metal ions among the possible coordination sites in the Cu(
ii
)-Ni(
ii
)-Aβ(1-16)Y10A and Cu(
ii
)-Ni(
ii
)-Zn(
ii
)-Aβ(1-16)Y10A systems have also been evaluated. It was found that the hexadecapeptide and its fragments are effective nickel(
ii
) binding ligands and complex formation processes of nickel(
ii
) ions are quite similar to those of copper(
ii
). Formation of mono- and di-nuclear complexes was detected in the nickel(
ii
)-Aβ(1-16)Y10A system suggesting the existence of two separated metal binding motifs: the N-terminus and internal histidyl residues. The preference for the coordination at the N-terminus was supported by the spectroscopic measurements but in equilibrium with the metal binding at the internal histidyl sites. Neither zinc(
ii
) nor nickel(
ii
) can, however, substitute copper(
ii
) in the mixed metal complexes of Aβ(1-16)Y10A, but both metal ions are able to alter the distribution of copper(
ii
) ions among the various binding sites. Both N-terminus (amino and His6) and internal histidyl residues (His13 and His14) can work as dinuclear binding motifs, preferably accommodating copper(II) and zinc(II), respectively, while nickel(
ii
) can occupy the remaining free coordination sites.
Neither zinc(
ii
) nor nickel(
ii
) can substitute copper(
ii
) in the complexes of Aβ(1-16)Y10A but both metal ions are able to alter the distribution of copper(
ii
) ions.