Far-UV Circular Dichroism experiments and Atomic Force Microscopy tomography are employed to assess the impact of β-sheet breaker on the Aβ(1−40) peptide aggregation process in the presence of Cu(II) or Zn(II) 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 Aβ(1−40) aggregation propensity, even in the presence of metal ions.

The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process / Stellato, Francesco; Fusco, Zelio; Chiaraluce, Roberta; Consalvi, Valerio; Dinarelli, Simone; Placidi, Ernesto; Petrosino, Maria; Rossi, Giancarlo; Minicozzi, Velia; Morante, Silvia. - In: BIOPHYSICAL CHEMISTRY. - ISSN 0301-4622. - STAMPA. - 229:(2017), pp. 110-114. [10.1016/j.bpc.2017.05.005]

The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process

CHIARALUCE, Roberta;CONSALVI, Valerio;Dinarelli, Simone;Placidi, Ernesto;PETROSINO, MARIA;
2017

Abstract

Far-UV Circular Dichroism experiments and Atomic Force Microscopy tomography are employed to assess the impact of β-sheet breaker on the Aβ(1−40) peptide aggregation process in the presence of Cu(II) or Zn(II) 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 Aβ(1−40) aggregation propensity, even in the presence of metal ions.
2017
amyloid-β peptide; fibrils; atomic force microscopy; circular dichroism; metalions; inhibitors
01 Pubblicazione su rivista::01a Articolo in rivista
The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process / Stellato, Francesco; Fusco, Zelio; Chiaraluce, Roberta; Consalvi, Valerio; Dinarelli, Simone; Placidi, Ernesto; Petrosino, Maria; Rossi, Giancarlo; Minicozzi, Velia; Morante, Silvia. - In: BIOPHYSICAL CHEMISTRY. - ISSN 0301-4622. - STAMPA. - 229:(2017), pp. 110-114. [10.1016/j.bpc.2017.05.005]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/955815
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