Metal loading capacity of Abeta N-terminus: a combined potentiometric and spectroscopic study of zinc(II) complexes with Abeta(1-16), its short or mutated peptide fragments and its polyethylene glycol-ylated analogue. (Articolo in rivista)

Type
Label
  • Metal loading capacity of Abeta N-terminus: a combined potentiometric and spectroscopic study of zinc(II) complexes with Abeta(1-16), its short or mutated peptide fragments and its polyethylene glycol-ylated analogue. (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/ic8006052 (literal)
Alternative label
  • Chiara A. Damante; Kataline Osz; Zoltan Nagy; Giuseppe Pappalardo; Giulia Grasso; Giuseppe Impellizzeri; Enrico Rizzarelli; Imre Sóvágó (2009)
    Metal loading capacity of Abeta N-terminus: a combined potentiometric and spectroscopic study of zinc(II) complexes with Abeta(1-16), its short or mutated peptide fragments and its polyethylene glycol-ylated analogue.
    in Inorganic chemistry
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Chiara A. Damante; Kataline Osz; Zoltan Nagy; Giuseppe Pappalardo; Giulia Grasso; Giuseppe Impellizzeri; Enrico Rizzarelli; Imre Sóvágó (literal)
Pagina inizio
  • 10405 (literal)
Pagina fine
  • 10415 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 48 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Chemical Sciences, University of Catania, V. le A. Doria 6, 95125 Catania, Italy, Department of Physical Chemistry, University of Debrecen, 4010 Debrecen, Hungary, Department of Inorganic and Analytical Chemistry, University of Debrecen, 4010 Debrecen, Hungary CNR Institute of Biostructures and Bioimaging, V. le A. Doria, 95125 Catania, Italy (literal)
Titolo
  • Metal loading capacity of Abeta N-terminus: a combined potentiometric and spectroscopic study of zinc(II) complexes with Abeta(1-16), its short or mutated peptide fragments and its polyethylene glycol-ylated analogue. (literal)
Abstract
  • Aggregation of the amyloid beta-peptide (Abeta) into insoluble fibrils is a key pathological event in Alzheimer's Disease (AD). There is now compelling evidence that metal binding to Abeta is involved in AD pathogenesis. The amino acid region 1-16 is widely considered as the metal binding domain of Abeta. In this work, we used a combined potentiometric, NMR, and electrospray ionization mass spectrometry (ESI-MS) approach to study the zinc(II) binding to a new polyethylene glycol (PEG)-conjugated peptide fragment encompassing the 1-16 amino acid sequence of Abeta (Abeta(1-16)PEG). Our results demonstrate for the first time that the Abeta(1-16) is able to coordinate up to three zinc ions, all the histidyl residues acting as independent anchor sites. The study was complemented by systematically investigating the zinc(II) complexes of a series of shorter peptide fragments related to the Abeta(1-16) sequence, namely, Abeta(1-4), Abeta(1-6), AcAbeta(1-6), AcAbeta(8-16)Y10A. The comparison of the whole results allowed the identification of the zinc(II) preferred binding sites within the longer Abeta(1-16) amino acid sequence. Unlike copper(II) that prefers the N-terminal amino group as the main binding site, the zinc(II) is preferentially placed in the 8-16 amino acidic region of Abeta(1-16). (literal)
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