Molecular dynamics simulations imply that the α-sheet structure is associated with toxic amyloid oligomers.
Alternating Cα chirality through strands confers α-sheet structure to peptides.
Peptides with alternating Cα chirality inhibit Aβ42, IAPP, and TTR aggregation.
Inhibitor potency correlates with the stability of α-sheet secondary structure.
Results identify new class of inhibitors against amyloidosis.