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 [10.1016/j.bpc.2017.05.005].
The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process
Stellato F.;Minicozzi V.
Writing – Original Draft Preparation
;Morante S.
2017-01-01
Abstract
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.| File | Dimensione | Formato | |
|---|---|---|---|
|
2017_BiophysChem.pdf
solo utenti autorizzati
Licenza:
Non specificato
Dimensione
551.63 kB
Formato
Adobe PDF
|
551.63 kB | Adobe PDF | Visualizza/Apri Richiedi una copia |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
