ArticleNature communications2021
Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 80 citations in OpenAlex.
- Antiamyloid Antibody Effects on Aβ-42 Protein Aggregates Profiled Using Nanospectroscopy.Chemical & biomedical imaging · 2026Article
- Infrared Near-Field Microscopy as a Platform for Nanoscale Biomedical Spectroscopy and Imaging.ACS applied materials & interfaces · 2026Review
- Changes in the concentration of phosphatidylcholine in lipid bilayers determines the aggregation rate of transthyretin.Biophysical chemistry · 2026Article
- Single-Oligomer Characterization of Tau Phosphorylation and Mechanical State.ACS measurement science au · 2025Article
- Nanochemical Cell-Surface Evaluation in Photothermal Spectroscopic Imaging of Antimicrobial Interactions in the Model SystemAnalytical chemistry · 2025Article
- Nanoscale Analysis beyond Imaging by Atomic Force Microscopy: Molecular Perspectives on Oncology and Neurodegeneration.Small science · 2025Review
- Effect of RNA on the supramolecular architecture of α-synuclein fibrils.Biophysical journal · 2025Article
- Detection of protein oligomers with nanopores.Nature reviews. Chemistry · 2025Review
- Single polyoxometalate-based nanoclusters characterized by infrared absorption nanospectroscopy.Communications chemistry · 2024Article
- Heterotypic Interactions of Amyloid β and the Islet Amyloid Polypeptide Produce Mixed Aggregates with Non-Native Fibril Structure.The journal of physical chemistry letters · 2024Article
- Accelerated Alzheimer's Aβ-42 secondary nucleation chronologically visualized on fibril surfaces.Science advances · 2024Article
- Nanoscale Structural Characterization of Amyloid β 1-42 Oligomers and Fibrils Grown in the Presence of Fatty Acids.ACS chemical neuroscience · 2024Article
- Elucidating the mechanisms of α-Synuclein-lipid interactions using site-directed mutagenesis.Neurobiology of disease · 2024Article
- Plasmalogens Alter the Aggregation Rate of Transthyretin and Lower Toxicity of Transthyretin Fibrils.The journal of physical chemistry letters · 2024Article
- Profiling native pulmonary basement membrane stiffness using atomic force microscopy.Nature protocols · 2024Article
- The influence of zwitterionic and anionic phospholipids on protein aggregation.Biophysical chemistry · 2024Review
- Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils.Communications biology · 2024Article
- Article
- Structural characterization of amyloid aggregates with spatially resolved infrared spectroscopy.Methods in enzymology · 2024Article
- Isotopic effects on in-plane hyperbolic phonon polaritons in MoONanophotonics (Berlin, Germany) · 2024Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 3 countries.
Funding
Abstract
Significant efforts have been devoted in the last twenty years to developing compounds that can interfere with the aggregation pathways of proteins related to misfolding disorders, including Alzheimer's and Parkinson's diseases. However, no disease-modifying drug has become available for clinical use to date for these conditions. One of the main reasons for this failure is the incomplete knowledge of the molecular mechanisms underlying the process by which small molecules interact with protein aggregates and interfere with their aggregation pathways. Here, we leverage the single molecule morphological and chemical sensitivity of infrared nanospectroscopy to provide the first direct measurement of the structure and interaction between single Aβ42 oligomeric and fibrillar species and an aggregation inhibitor, bexarotene, which is able to prevent Aβ42 aggregation in vitro and reverses its neurotoxicity in cell and animal models of Alzheimer's disease. Our results demonstrate that the carboxyl group of this compound interacts with Aβ42 aggregates through a single hydrogen bond. These results establish infrared nanospectroscopy as a powerful tool in structure-based drug discovery for protein misfolding diseases.
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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.