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

•The effect of Cu(II)/Zn(II) ions and β-sheet breakers on Aβ1-40 fibril formation•CD spectroscopy and AFM monitor secondary structure changes and fibril formation•No β-sheet structure transition and no fibrils in the presence of β-sheet breakers•β-Sheet breakers peptides prevent fibril formation in the presence of metal ions.

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.

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