Fig. 3

Half maximal effective concentration (EC50) of anti-Aβ antibody dose-response curves against three different Aβ42 forms. Antibody binding was measured using a direct ELISA against immobilised antigen, and the EC50 taken from a 4-parameter logistic equation fitted to the experimental data. Here, “M” denotes monomeric non-aggregated peptide, “O” oligomeric forms of the peptide with anti-parallel orientation of the β-sheets (see Additional Figure 7 in the Supplemental Appendix) and an oligomer content of 94% with an average Mw of 702 ± 4 kDa as determined by SEC-MALS (see Additional Figure 2 in the Supplemental Appendix), and “F” fibrillar forms of the peptide with a parallel orientation of the β-sheets (see Additional Figure 7 in the Supplemental Appendix) for which the Mw is unknown. All ELISAs were carried out in duplicates except for ALZ-201 and chALZ-201 against Aβ42CC O, for which n=68 and n=18, respectively. #: No binding detected. The error is the standard deviation (SD). See Additional Figure 8 in the Supplemental Appendix for experimental data