Figure 1
Figure 1. Aβ22-41 binds to fibrinogen and fragment D. (A-B) Biotin-labeled Aβ42, Aβ1-16, Aβ15-25, and Aβ22-41 were incubated with fibrinogen (FBG) or fragment D (FD), and pulldown assays were carried out using streptavidin-coated magnetic beads. All samples were analyzed by western blot in unreduced condition using an anti-fibrinogen antibody. Only Aβ22-41 showed binding to both fibrinogen (A) and fragment D (B). When no Aβ peptides were added, the level of bound fibrinogen or fragment D was negligible. Images and graphs are representative of 4 experiments. (C-D) The binding between biotin-labeled Aβ42 or Aβ fragments with fibrinogen or fragment D was determined by AlphaLISA (n = 3). Controls and other lanes in panel A are from the same gel with some lanes omitted for clarity. Results presented in graphs are mean ± standard error of the mean (SEM).

Aβ22-41 binds to fibrinogen and fragment D. (A-B) Biotin-labeled Aβ42, Aβ1-16, Aβ15-25, and Aβ22-41 were incubated with fibrinogen (FBG) or fragment D (FD), and pulldown assays were carried out using streptavidin-coated magnetic beads. All samples were analyzed by western blot in unreduced condition using an anti-fibrinogen antibody. Only Aβ22-41 showed binding to both fibrinogen (A) and fragment D (B). When no Aβ peptides were added, the level of bound fibrinogen or fragment D was negligible. Images and graphs are representative of 4 experiments. (C-D) The binding between biotin-labeled Aβ42 or Aβ fragments with fibrinogen or fragment D was determined by AlphaLISA (n = 3). Controls and other lanes in panel A are from the same gel with some lanes omitted for clarity. Results presented in graphs are mean ± standard error of the mean (SEM).

Close Modal

or Create an Account

Close Modal
Close Modal