Far-UV Circular Dichroism experiments and Atomic Force Microscopy tomography are employed to assess the impact of beta-sheet breakers on the A?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 ?-sheet breakers are effective in reducing the A?1-40 aggregation propensity, even in the presence of metal ions.
The effect of beta-sheet breaker peptides on metal associated Amyloid-? peptide aggregation process
Dinarelli S;Placidi E;Placidi E;
2017
Abstract
Far-UV Circular Dichroism experiments and Atomic Force Microscopy tomography are employed to assess the impact of beta-sheet breakers on the A?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 ?-sheet breakers are effective in reducing the A?1-40 aggregation propensity, even in the presence of metal ions.File in questo prodotto:
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