Title
The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process
Author
F. Stellato, Z. Fusco, R. Chiaraluce, V. Consalvi, S. Dinarelli, E. Placidi, M. Petrosino, G.C. Rossi, V. Minicozzi, S. Morante
Year
2017
Journal
Biophysical Chemistry
Abstract
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.
Instrument
J-720
Keywords
Circular dichroism, Secondary structure, Ligand binding, Aggregation, Biochemistry