Fig. 1. Rational identification of a peptide ligand for αS toxic species.
a Main molecular features of the four isolated α-synuclein (αS) species. Values with a dagger (†) represent extrapolations based on the average number of monomers in each species. In the upper schemes of αS oligomeric and fibrillar species, the acidic C-terminal region is not depicted since it has been described to be in a disordered and conformationally flexible state21–23. b Helical wheel projection of PSMα3 sequence (red, hydrophobic residues; blue pallet, hydrophilic residues depending on their character). c Surface representation of the three-dimensional structure of PSMα3 with hydrophobic residues in red and hydrophilic residues in blue. d Far-UV circular dichroism spectra of PSMα3.