Fig. 8
From: Aβ43 aggregates exhibit enhanced prion-like seeding activity in mice
Conformational characterization of recombinant Aβ aggregates. a Schematic of the formation conditions for recombinant Aβ aggregates. b Fluorescence emission spectra (left panel) for curcumin bound to recombinant Aβ38 (green), Aβ40 (blue), Aβ42 (black), and Aβ43 (red) aggregates. The curcumin λmax values (right panel) for Aβ38 aggregates were significantly higher than for the other Aβ variants (P = 0.016 vs. Aβ40, P = 0.014 vs. Aβ42, and P = 0.016 vs. Aβ43 by one-way ANOVA followed by Tukey’s multiple comparisons test). Data is mean ± s.e.m for 4 biologically independent aggregate preparations. c Fluorescence emission spectra for hFTAA bound to recombinant Aβ38 (green), Aβ40 (blue), Aβ42 (black), and Aβ43 (red) aggregates. Data is mean ± s.e.m for 2–3 biologically independent aggregate preparations. d Immunoblots (6E10 antibody) of the insoluble fraction following exposure of recombinant Aβ aggregates to the indicated concentrations of proteinase K (PK). e Conformational stability assays for recombinant Aβ aggregates. Representative Aβ immunoblots (left panel; 6E10 antibody) and the resultant denaturation curves (right panel) are shown. The curves depict mean residual insoluble Aβ values ± s.e.m. following treatment with the indicated concentrations of GdnHCl, and the calculated [GdnHCl]50 values are shown. n = 3 biologically independent aggregate preparations per Aβ variant