Figure 7
(A–D) Aβ43 (5 μM) was incubated with agitation for 0–8 h at 25°C in the absence (open circles) or presence of 5 μM (filled triangles), 10 μM (filled squares) or 20 μM (filled circles) (Arg-Benz)4-CONH2 (A), (Arg-Sal)3-(Cit-Sal)-CONH2 (B), Sal-(Lys-Sal)3-CONH2 (C) or Ac-Sal-(Lys-Sal)3-CONH2 (D). Aβ43 fibrillization was assessed by ThT fluorescence. Values represent means±S.E.M. (n=3). (E) Aβ43 (5 μM) was incubated with agitation for 4 h at 25°C in the absence or presence of the indicated foldamer (10 μM). Aβ43 fibrillization was assessed by EM. Scale bar, 500 nm.
(Arg-Benz)4-CONH2 and (Arg-Sal)3-(Cit-Sal)-CONH2 inhibit spontaneous Aβ43 fibrillization

(AD) Aβ43 (5 μM) was incubated with agitation for 0–8 h at 25°C in the absence (open circles) or presence of 5 μM (filled triangles), 10 μM (filled squares) or 20 μM (filled circles) (Arg-Benz)4-CONH2 (A), (Arg-Sal)3-(Cit-Sal)-CONH2 (B), Sal-(Lys-Sal)3-CONH2 (C) or Ac-Sal-(Lys-Sal)3-CONH2 (D). Aβ43 fibrillization was assessed by ThT fluorescence. Values represent means±S.E.M. (n=3). (E) Aβ43 (5 μM) was incubated with agitation for 4 h at 25°C in the absence or presence of the indicated foldamer (10 μM). Aβ43 fibrillization was assessed by EM. Scale bar, 500 nm.

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