Far-UV Circular Dichroism experiments and Atomic Force Microscopy tomography are employed to assess the impact of β-sheet breakers on the Aβ peptide aggregation process in the presence of Cu or Zn 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 aggregation propensity, even in the presence of metal ions.
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| http://dx.doi.org/10.1016/j.bpc.2017.05.005 | DOI Listing |
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