ArticleNature chemical biology2023
Structural mechanism for specific binding of chemical compounds to amyloid fibrils.
Article in Nature chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 72 citations in OpenAlex.
- Three Distinct Binding Modes Govern High-Affinity Ligand Interactions with Amyloid Fibrils.Biochemistry · 2026Article
- Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control.Journal of the American Chemical Society · 2026Article
- A Covalent Resveratrol-Polyoxometalate Hybrid for Synergistic Disassembly of Prion Protein Fragment 106-126 Aggregates and Catalytic Scavenging of Reactive Oxygen Species.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Structure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathies.Molecular systems biology · 2026Article
- Structures of dye-bound transthyretin amyloid fibrils from abdominal fat biopsies.Nature communications · 2026Article
- Unraveling Alzheimer's complexity with a distinct AβNature chemical biology · 2026Article
- Fluorescent Labeling Methods for Brain Structure Research.Molecules (Basel, Switzerland) · 2026Review
- Interactions Between Nutraceuticals and α-Synuclein Conformational States: Molecular Mechanisms and Neuroprotective Implications in Parkinson's Disease.International journal of molecular sciences · 2026Review
- Structural and Functional Determinants of ARIA-H Risk in Anti-Amyloid Monoclonal Antibodies: A Comparative Mechanistic Framework for Alzheimer's Immunotherapy Development.Current neuropharmacology · 2026Article
- Article
- Interactions of Neurodegenerative Disease Positron Emission Tomography Imaging Probe Candidates with the C-Terminus of α-Synuclein Fibrils.Chembiochem : a European journal of chemical biology · 2025Article
- FibrilPaint to determine the length of Tau amyloids in fluids.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Anle138b binds predominantly to the central cavity in lipidic Aβ₄₀ fibrils and modulates fibril formation.Nature communications · 2025Article
- De novo design of protein binders to stabilize monomeric TDP-43 and inhibit its pathological aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Alpha-synuclein fibril structures cluster into distinct classes.Biophysical journal · 2025Review
- Design of Ig-like binders targeting α-synuclein fibril for mitigating its pathological activities.Nature communications · 2025Article
- A Cooperative Model for Symmetric Ligand Binding to Protein Fibrils.Biochemistry · 2025Article
- In silico identification of substrate-binding sites in type-1A α-synuclein amyloids.Biophysical journal · 2025Article
- High-Throughput Screening of Amyloid Inhibitors via Covalent-Labeling Mass Spectrometry.Analytical chemistry · 2025Article
- Ligands for Protein Fibrils of Amyloid-β, α-Synuclein, and Tau.Chemical reviews · 2025Review
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibril is an important pharmaceutical target for diagnostic and therapeutic treatment of neurodegenerative diseases. However, rational design of chemical compounds that interact with amyloid fibrils is unachievable due to the lack of mechanistic understanding of the ligand-fibril interaction. Here we used cryoelectron microscopy to survey the amyloid fibril-binding mechanism of a series of compounds including classic dyes, (pre)clinical imaging tracers and newly identified binders from high-throughput screening. We obtained clear densities of several compounds in complex with an α-synuclein fibril. These structures unveil the basic mechanism of the ligand-fibril interaction, which exhibits remarkable difference from the canonical ligand-protein interaction. In addition, we discovered a druggable pocket that is also conserved in the ex vivo α-synuclein fibrils from multiple system atrophy. Collectively, these findings expand our knowledge of protein-ligand interaction in the amyloid fibril state, which will enable rational design of amyloid binders in a medicinally beneficial way.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.