Science Advances

Supplementary Materials

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  • fig. S1. Influence of these metal complexes on the fluorescence of ECFP (a non-Aβ fusion system).
  • fig. S2. The influence of these metallohelices on the fluorescence of ThT.
  • fig. S3. Aggregation kinetics of Aβ42 monitored by ThT assay in the absence or presence of A1 and B4.
  • fig. S4. Aggregation kinetics of Aβ40 monitored by ThT assay in the absence or presence of the ligands of A1 and B4.
  • fig. S5. The inhibition effect of A1 and B4 on Aβ40/Aβ42 fibrillogenesis at different concentrations.
  • fig. S6. The inhibition effect of the metallohelices on Aβ40 aggregation measured by SDS-PAGE.
  • fig. S7. The influence of A1 and B4 on the second structures of Aβ42 monitored by CD.
  • fig. S8. Fluorescence titration of Aβ40 (3 μM) with various concentrations of metallohelices in 20 mM tris buffer.
  • fig. S9. ITC data for the Aβ40 titrations with metallohelices.
  • fig. S10. SDS-PAGE analysis of the effect of metallohelices on tryptic digests of Aβ12–28.
  • fig. S11. The aggregation kinetics of Aβ25–35 was monitored by the fluorescence of ThT in the absence or presence of A1 and B4.
  • fig. S12. FTIR spectra of Aβ40 in different conditions.
  • fig. S13. Structures of Aβ40 and metallohelices used for docking study.
  • fig. S14. Energy-minimized average models of A1 with Aβ40 interactions.
  • fig. S15. A1 and B4 scavenging ROS monitored by NBT and ABTS methods.
  • fig. S16. Cyclic voltammograms corresponding to the O2/O2 redox couple.
  • fig. S17. Effect of the metallohelices on ROS production in PC12 cells.
  • fig. S18. Absorption spectra of 5 μM metallohelices in water and PBS.
  • fig. S19. Effect of A1 and B4 on PC12 cell viability determined by MTT.
  • fig. S20. Protection effects of metallohelices on Aβ40- and Aβ42-induced cytotoxicity of PC12 cells.
  • table S1. IC50 values of metallohelices A1 and B4 for the inhibition of fibril formation and destabilization of the preformed fibrils.
  • table S2. Analysis of fluorescence titration and ITC data.
  • table S3. Enthalpy (ΔH), entropy (ΔS), and Gibbs free energy (ΔG) of the binding of Aβ with metallohelices at pH 7.3.

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