Aluminum-triggered structural modifications and aggregation of beta-amyloids. (Articolo in rivista)

Type
Label
  • Aluminum-triggered structural modifications and aggregation of beta-amyloids. (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1007/s00018-005-5141-0 (literal)
Alternative label
  • Ricchelli F.; Drago, D.; Filippi, B.; Tognon, G.; Zatta, P. (2005)
    Aluminum-triggered structural modifications and aggregation of beta-amyloids.
    in Cellular and molecular life sciences (Print. ed.)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ricchelli F.; Drago, D.; Filippi, B.; Tognon, G.; Zatta, P. (literal)
Pagina inizio
  • 1 (literal)
Pagina fine
  • 10 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 62 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 15 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Tecnologie Biomediche - CNR - Sezione di Padova (literal)
Titolo
  • Aluminum-triggered structural modifications and aggregation of beta-amyloids. (literal)
Abstract
  • We investigated the structural effects induced by Al3+ on different b-amyloid (Ab) fragments at pH 7.4 and T= 25°C, with particular attention given to the sequences 1-40 and 1-42. Al3+ caused peptide enrichment in b sheet structure and formation of solvent-exposed hydrophobic clusters. These intermediates evolved to polymeric aggregates which organized in fibrillar forms in the case of the Al3+-Ab(1-42) complex. Comparative studies showed that Zn2+ and Cu2+ were much less efficient than Al3+ in stimulating the spontaneous aggregation/fibrillogenesis of Abs. Studies with liposomes as membrane models showed dramatic changes in the structural properties of the lipid bilayer in the presence of Al3+-Ab complexes, suggesting a major role of Al3+ in Ab-induced cell dysfunction. Al3+ effects were abolished by desferrioxamine mesylate (DFO) only in solution. We concluded that, in vivo, DFO may act as a protective agent by preventing or reverting Ab aggregation in the extracellular spaces. (literal)
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