Competitive Mirror Image Phage Display Derived Peptide Modulates Amyloid Beta Aggregation and Toxicity
Fig 3
The relative binding affinity of single phage clones from mirror image phage display (clone numbers 6.xx) and a previously conducted mirror image phage display (clone numbers 5.xx) to SEC-derived biotinylated Aβ1–42 monomers, oligomers and fibrils as well as the non-coated wells was analyzed. The M13 phage-specific antibody was used for detection. Transformation of substrate by the antibody-conjugated HRP was measured at 450 nm. Amplified single phage clones were added to wells coated with 150 ng Aβ1–42 monomers (red) or 150 ng Aβ1–42 oligomers and fibrils (1:1; green) or to wells only coated with streptavidin (blue). Cross reactivity of the M13 phage-specific antibody was tested in an approach without addition of phages. After background subtraction of the anti M13 antibody values, the values for phage to Aβ1–42 oligomer/fibril binding were normalized to the values of phage to Aβ1–42 monomer binding according to the outcome of coating efficiency controls with the Aβ specific antibody 6E10.