ArticleJournal of applied crystallography2025
Differentiating the solution structures and stability of transthyretin tetramer complexed with tolcapone and tafamidis using SEC-SWAXS and NMR.
Article in Journal of applied crystallography, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Tolcapone Interferes With Key Pathological Features in Alzheimer's Disease.Bioinorganic chemistry and applications · 2026Article
- Introduction to the special issue related to the 19th International Small Angle Scattering Conference (SAS2024).Journal of applied crystallography · 2025Article
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Authors and funding
8 authors.
Funding
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Abstract
Human transthyretin (TTR) is a homotetrameric protein involved in transporting thyroxine (T4) and retinol-binding protein within serum and cerebrospinal fluid. The disassociation of TTR's tetrameric structure can lead to the formation of biologically toxic TTR amyloid fibrils. Tolcapone, a small molecule currently under clinical trial, has shown potential as a TTR stabilizer and may act as an alternative to tafamidis, the conventional therapeutic agent used to prevent TTR dissociation. Using size-exclusion-chromatography-based small- and wide-angle X-ray scattering (SEC-SWAXS) complemented by nuclear magnetic resonance (NMR) spectroscopy, this study reveals the solution conformations of Apo-TTR and TTR complexed with tolcapone and tafamidis. Our results indicate that both compounds can bind similarly to the two T4 sites of TTR, leading to a small increase in the radius of gyration from 24.3 ± 0.1 Å (Apo-TTR) to 25.8 ± 0.1 Å. Consequently, both compounds largely stabilize the TTR against dissociation, denaturation and oligomerization up to 8
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