Fig. 7: Sequence alterations in P1 do not result in aggregation of γSyn.
From: Single residue modulators of amyloid formation in the N-terminal P1-region of α-synuclein
a Sequence alignment of αSyn and γSyn focussing on the P1 region (boxed). Residues that differ are highlighted with red arrows and labels. Aggregation kinetics for b WT αSyn, c WT γSyn, d γSyn M38L, e γSyn A42S and f γSyn M38L/A42S. In each case the relevant residue in γSyn is replaced with the equivalent residue in αSyn, demonstrating that these amino acid substitutions do not induce amyloid formation under these conditions (20 mM Tris-HCl, pH 7.5, 200 mM NaCl, 37 °C, 600 rpm shaking). Seeded data (with WT αSyn seeds) are shown in Supplementary Fig. 9. The insets show representative TEM images of each sample taken at the end of the reaction (110 h) of one biological replicate (n = 2). % pellet are shown in Supplementary Table 1e. Source data are provided as a Source Data file.
