Aß(25-35) and its C-and/or N-blocked derivatives: copper driven structural features and neurotoxicity. (Articolo in rivista)

Type
Label
  • Aß(25-35) and its C-and/or N-blocked derivatives: copper driven structural features and neurotoxicity. (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/jnr.21135 (literal)
Alternative label
  • Maria Laura Giuffrida; Giulia Grasso; Menotti Ruvo; Carlo Pedone; Angela Saporito; Daniela Marasco; Bruno Pignataro; Claudia Cascio; Agata Copani; Enrico Rizzarelli (2007)
    Aß(25-35) and its C-and/or N-blocked derivatives: copper driven structural features and neurotoxicity.
    in Journal of neuroscience research; John Wiley & sons, Inc., Hoboken (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Maria Laura Giuffrida; Giulia Grasso; Menotti Ruvo; Carlo Pedone; Angela Saporito; Daniela Marasco; Bruno Pignataro; Claudia Cascio; Agata Copani; Enrico Rizzarelli (literal)
Pagina inizio
  • 623 (literal)
Pagina fine
  • 633 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 85 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • PhD Program in Neurobiology, Faculty of Medicine, University of Catania, Catania, Italy I.B.B., CNR, Catania, Italy I.B.B., CNR, Napoli, Italy Department of Physical-Chemistry (F. Accascina), University of Palermo, Palermo, Italy Consorzio Catania Ricerche, Catania, Italy Department of Pharmaceutical Sciences, University of Catania, Catania, Italy Department of Chemical Sciences, University of Catania, Catania, Italy (literal)
Titolo
  • Aß(25-35) and its C-and/or N-blocked derivatives: copper driven structural features and neurotoxicity. (literal)
Abstract
  • The toxic properties of b-amyloid protein, Ab(1-42), the major component of senile plaques in Alzheimer's disease, depend on nucleation-dependent oligomerization and aggregation. In addition, Ab(1-42) toxicity is favored by the presence of trace metals, which affect the secondary structure of the peptide. A peptide comprising 11 residues within Ab(1-42) [Ab(25-35)] aggregates and retains the neurotoxic activity of Ab(1-42). We have used both Ab(25-35) and its C-amidated or N-acetylated/C-amidated derivatives to investigate the role of copper(II) in modulating the conformation and aggregation state as well as the neurotoxic properties of amyloid peptides. Electrospray ionization mass spectrometry (ESI-MS) and electron paramagnetic resonance (EPR) measurements were performed to verify the formation of copper(II)/Ab(25-35) complexes and to determine the coordination mode, respectively. Ab(25- 35) and its derivatives were analyzed by circular dichroism spectroscopy to assess their secondary structure, subjected to thioflavine-T (Th-T) binding assay to reveal b-sheet structured aggregates formation, and imaged by scanning force microscopy. Toxicity was assessed on mature cultures of rat cortical neurons. We found that b-sheet-structured species of Ab(25-35) were neurotoxic, whereas the random-coil-structured derivatives were devoid of effect. Interestingly, copper promoted the random-coil/b-sheet transition of Ab(25-35), with ensuing peptide toxicity, but it induced the toxicity of the N-acetylated/C-amidated derivative without affecting peptide folding. Moreover, copper did not influence either the folding or the activity of the C-amidated Ab(25-35), suggesting that blockade of the C-terminus of Ab peptides might be sufficient to prevent Ab toxicit (literal)
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