Extended Data Fig. 4: Detection of the aggregates composed of Aβ and tau fragments by ESI–MS.
From: Interactions with tau’s microtubule-binding repeats modulate amyloid-β aggregation and toxicity
a, Deconvoluted MS spectra of Aβ40 with R4 or PHF6*. The peaks obtained by the mass-to-charge ratio of Aβ40 with R4 or PHF6* are presented in Supplementary Fig. 18. Hetero-assemblies of Aβ40 with R4 or PHF6* with the different Aβ40-to-tau fragment stoichiometry are displayed with diamonds. b, Relative abundance of Aβ40 species unbound and bound with R4 or PHF6* calculated by integrating the characterized peaks from the deconvoluted mass by UniDec57. Conditions: [Aβ40] = 10 μM; [tau fragment] = 10, 50, and 100 μM; 20 mM ammonium acetate, pH 7.4; 1 h; 37 °C; 250 rpm. All values are indicated as mean ± s.e.m. for n = 3 examined over three independent experiments. *Values of the relative abundance of heterogeneous oligomers of Aβ40 species with PHF6* could not be determined because they were not observed under our experimental conditions.
