http://www.cnr.it/ontology/cnr/individuo/prodotto/ID13790
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
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- 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)
- Editore
- Prodotto di
- Autore CNR
- Insieme di parole chiave
Incoming links:
- Autore CNR di
- Prodotto
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
- Editore di
- Insieme di parole chiave di