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. 2021 Nov 29;41(2):e108591. doi: 10.15252/embj.2021108591

Figure 1. Differential binding of Aβ‐aggregating species in Aβ cellulose peptide microarrays.

Figure 1

  • A
    Aβ1‐42 sliding window membrane setup. Red indicates where the KLVFFA starts presented whole. Green where GAIIGL presented whole. Blue indicates the controls (4 proline breakers, 5 scrambled Aβ peptides, sequences Appendix Table S1).
  • B
    SEC‐MALS of Biot‐Aβ1‐42 preparation with 7 M GnHCL showing a clear monomeric peak and a smaller oligomeric.
  • C
    100 nM of Biot‐Aβ1‐42 monomers show no binding on membrane (down panel), TEM image shows no aggregating species in the sample (upper panel). Scale bar: 500 nm.
  • D
    Void fraction (oligomers) shows strong binding on first APR of Aβ1‐42. Scale bar: 500 nm.
  • E
    Normalized ThT kinetics of 10 μM Biot‐Aβ1‐42 with timepoints of samples that incubated with Aβ1‐42 membranes.
  • F–H
    Binding of different aggregating samples to Aβ membranes and their TEM images. 100 nM of sample1 (early oligomers) binds strongly to middle APR (F), 100 nM of sample 2 (late oligomers) binds in both middle and C‐terminal APR of Aβ1‐42 (down panel) while TEM images show fibrillar structures (upper panel) (G), 100 nM of sample 3 shows no specific binding to Aβ1‐42 membranes (H). Scale bars: 500 nm.
  • I
    ThT kinetics of Biot‐Aβ1‐42 seeding. 10 μM of Biot‐Aβ1‐42 incubated with 0.5 or 1 μM of Biot‐Aβ1‐42 seeds.
  • J
    100 nM of Biot‐Aβ1‐42 seeds show a strong binding in both APRs. TEM image (upper panel) slow clear fragmentation of fibrils. Scale bar: 1 μm.