fig3

Figure 3. Small molecule to stabilize amyloid monomer and divert to off-pathway aggregates. (A) Tafamidis-mediated stabilization of TTR in plasma obtained from patients with wild-type (WT), V30M, and V122I alleles. Figure reproduced from Bulawa et al.^[30]. (B) Crystal structure depicting the binding of tafamidis to TTR (PDB ID: 3TCT). The four TTR monomers are shown in distinct colors. Figure reproduced with permission from Bulawa et al.^[30]. (C) Electron microscopy analysis comparing the aggregation reactions of Aβ₄₂ with and without EGCG treatment. Figure reproduced from Ehrnhoefer et al.^[36]. (D, E) Evaluation of the impact of EGCG on Aβ₄₂ aggregation using ThT fluorescence measurements. (D) SDS-PAGE assays. (E) Reproduced from Ehrnhoefer, et al.^[36]. (F) Inhibition of Aβ aggregation by CLR01. The impact of CLR01 on Aβ₄₀ aggregation was evaluated using ThT fluorescence measurements and electron microscopy. The data was reproduced with permission from Sinha et al.^[40]. (G) Identification of CLR01 binding sites on Aβ through solution-state NMR analysis. Figure reproduced with permission from Sinha et al.^[40]. EGCG: Epigallocatechin gallate; NMR：nuclear magnetic resonance; SDS-PAGE: sodium dodecyl sulfate polyacrylamide gel electrophoresis; TTR: transthyretin.