Fig. 2
From: Amyloid fibril proteomics of AD brains reveals modifiers of aggregation and toxicity
Amyloid fibril cores are enriched with Aβ42 and Aβ38 peptides. a WB analysis across indicated fractions from AppNL−G−F/NL−G−F mouse cortical extracts with Aβ40, Aβ42, and Aβ38 specific antibodies. A11, LOC blots, and Coomassie brilliant blue staining indicate abundance of oligomers, fibrils and total protein, respectively. Red asterisks indicate HMW aggregates. b-d Absolute quantification of Aβ40, Aβ42 and Aβ38 peptides in purified SDS-resistant amyloid fibrils from cortical extracts of App KI (AppNL/NL, AppNL−F/NL−F, and AppNL−G−F/NL−G−F) and 5xFAD mice using sandwich ELISAs. e, f Dot blot and WB analysis of fibril cores obtained from postmortem AD brain tissues using antibodies for Aβ40, Aβ42 and Aβ38. Ponceau S-stained membrane in (e) was used for visualization of loading protein amount. g-i Absolute quantification of Aβ40, Aβ42 and Aβ38 peptides in purified fibrils from AD human brains. Fifteen amyloid samples from each indicated group were analyzed. Data in b-d and g-i are mean ± SEM; *, p-value < .05; **, p-value < .01; ***, p-value < .001; analyzed with unpaired Student’s t-test or one-way ANOVA with post hoc Sidak test. P = pellet, and S = supernatant. NL = AppNL/NL, NL-F = AppNL−F/NL−F, NL-G-F = App.NL−G−F/NL−G−F. N = 3 mice (a), 10 (b-d); N = 3 humans (e–f), 15 (g-i)