Far-UV Circular Dichroism experiments and Atomic Force Microscopy tomography are employed to assess the impact of β-sheet breakers on the Aβ1-40 peptide aggregation process in the presence of Cu2+ or Zn2+ transition metals. In this work we focus on two specific 5-amino acids long β-sheet breakers, namely the LPFFD Soto peptide, already known in the literature, and the LPFFN peptide recently designed and studied by our team. We provide evidence that both β-sheet breakers are effective in reducing the Aβ1-40 aggregation propensity, even in the presence of metal ions.
Stellato, F., Fusco, Z., Chiaraluce, R., Consalvi, V., Dinarelli, S., Placidi, E., et al. (2017). The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process. BIOPHYSICAL CHEMISTRY, 229, 110-114.
Tipologia: | Articolo su rivista |
Citazione: | Stellato, F., Fusco, Z., Chiaraluce, R., Consalvi, V., Dinarelli, S., Placidi, E., et al. (2017). The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process. BIOPHYSICAL CHEMISTRY, 229, 110-114. |
Lingua: | English |
Settore Scientifico Disciplinare: | Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin) |
Revisione (peer review): | Esperti anonimi |
Tipo: | Articolo |
Rilevanza: | Rilevanza internazionale |
Digital Object Identifier (DOI): | http://dx.doi.org/10.1016/j.bpc.2017.05.005 |
Stato di pubblicazione: | Pubblicato |
Data di pubblicazione: | 2017 |
Titolo: | The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process |
Autori: | |
Autori: | Stellato, F; Fusco, Z; Chiaraluce, R; Consalvi, V; Dinarelli, S; Placidi, E; Petrosino, M; Rossi, GC; Minicozzi, V; Morante, S |
Appare nelle tipologie: | 01 - Articolo su rivista |
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