Fig. 6: αSyn aggregation rate is dependent on the identity of residue 38.

a Sequence alignment showing that the P1 regions of αSyn and γSyn differ at two positions, residues 38 and 42. Aggregation kinetics of b γSyn, c αSyn L38A (reproduced for clarity from Fig. 5b), and d αSyn L38M. The inset shows seeding of L38M with 10% (w/w) preformed WT αSyn seeds. e TEM images of αSyn L38M incubated in the absence (left hand side) or presence (right hand side) of 10% (w/w) preformed seeds of WT αSyn. f, g AFM image and height/length distribution analysis (n = 2167 objects analysed in one image) of the products of incubation of L38M (without seeds). Amyloid formation kinetics (h) and TEM images (i left hand side) for αSyn L38I incubated without seeds. The inset shows seeding of L38I with 10 % (w/w) preformed WT αSyn seeds, with the TEM image alongside (i right hand side). TEM images of each sample taken at the end of the reaction (110 h) of one biological replicate (n = 2) All reactions were carried out at pH 7.5, 200 mM NaCl, 37 °C, shaking (600 rpm) (de novo growth) or quiescent (seeded growth) each using 100 μM αSyn. See also Supplementary Fig. 8. % pellet and t₅₀ values are shown in Supplementary Table 1d. Source data are provided as a Source Data file.