Stellato, FFusco, ZelioChiaraluce, RConsalvi, VDinarelli, SPlacidi, EPetrosino, MRossi, G CMinicozzi, VMorante, S2020-04-060301-4622http://hdl.handle.net/1885/202749Far-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.5 pagesapplication/pdfen-AU© 2017 Elsevier B.V.Amyloid-β peptide, Fibrils, Atomic Force Microscopy, Circular Dichroism, Metal ions, Inhibitor2017-1010.1016/j.bpc.2017.05.0052019-11-25