Binding of 2A4 to ALκ Hig amyloid extract and rV_λ6Wil fibrils in the presence of different Bence Jones proteins.

<p>(A) ALκ amyloid extract, 10 µg/mL Hig, L (blue) or 0.83 µM rV_λ6Wil fibrils (red) were dried onto the wells of a 96-well microplate and the binding of 2A4 evaluated in the presence of BJp pre-incubated with 2A4. Concentrations of 2A4 were 5 nM for wells containing rV_λ6 Wil (red) and 200 nM for the Hig samples (blue). Competitor BJps, designated on the abscissa by 3 letter code were present at 41.5 µM. The data are expressed as the % of the positive control, i.e., mAb 2A4 in the absence of any BJp. Competition with rV_λ6 Wil fibrils (far right) served as a positive control. (B) EuLISA titration of 2A4 on Hig, L amyloid extract, 10 µg/mL (closed) and rV_λ6 Wil fibrils, 0.25 µM (open). The EC₅₀ for Wil was ∼3 nM and for Hig, ∼40 nM.