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

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.