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

Stellato, F; Fusco, Zelio; Chiaraluce, R; Consalvi, V; Dinarelli, S; Placidi, E; Petrosino, M; Rossi, G C; Minicozzi, V; Morante, S

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

Date

2017-10

Authors

Stellato, F

Fusco, Zelio

Chiaraluce, R

Consalvi, V

Dinarelli, S

Placidi, E

Petrosino, M

Rossi, G C

Minicozzi, V

Morante, S

Publisher

Elsevier

Abstract

Far-UV Circular Dichroism experiments and Atomic Force Microscopy tomography are employed to assess the impact of beta-sheet breakers on the A beta(1-40) peptide aggregation process in the presence of Cu2+ or Zn2+ transition metals. In this work we focus on two specific 5-amino acids long beta-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 13 -sheet breakers are effective in reducing the A beta(1-40) aggregation propensity, even in the presence of metal ions.