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. 2022 Aug 30;25(9):1134–1148. doi: 10.1038/s41593-022-01140-3

Extended Data Fig. 1. Related to main Fig. 1.

Extended Data Fig. 1

(ai) α-Syn-AF488-monomer or α-Syn-AF594-monomer alone did not induce a FRET signal. (aii) FRET was not induced by 594 nm excitation. (b) Time-lapse representative images of FRET showing intracellular localization of α-Syn assemblies after adding AF488-α-Syn and AF-594-α-Syn monomers to the media. (ci & ii) Intracellular FRET signal induced by WT α-Syn (ci; oligomer, cii; monomer) occurred in a concentration- and time-dependent manner (n = 3 independent experiments). The minimum concentration to induce FRET within 72 hours was 5 nM oligomer; the minimum monomer concentration to induce FRET at 72 hours was 50 nM, whilst 500 nM monomer induced a FRET signal within 3 hours (di & ii) FRET signal colocalized with an amyloid oligomer-specific aptamer and partially with an α-Syn filament antibody. (diii) Co-localization was quantified using Mander’s ratio (n = 3 independent experiments). Note. Data are represented as Data ± SEM (box). *#p < 0.05, **##p < 0.005, ***###p < 0.0005. Detailed statistical information is provided in Supplementary Table 1.

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