ArticleMolecules (Basel, Switzerland)2020
Characterization by Nano-Infrared Spectroscopy of Individual Aggregated Species of Amyloid Proteins.
Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Investigating Structural Heterogeneities of Amyloid Aggregates with Spatially Resolved Infrared Spectroscopy.Accounts of chemical research · 2026Article
- Hydration water dynamics in amyloid-β aggregates using deuterium and oxygen-17 solid-state NMR spectroscopy.The Journal of chemical physics · 2026Article
- Antiamyloid Antibody Effects on Aβ-42 Protein Aggregates Profiled Using Nanospectroscopy.Chemical & biomedical imaging · 2026Article
- Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025Review
- Structural diversity of Alzheimer-related protein aggregations revealed using photothermal ratio-metric micro-spectroscopy.Biomedical optics express · 2024Article
- Review
- AFM-IR for Nanoscale Chemical Characterization in Life Sciences: Recent Developments and Future Directions.ACS measurement science au · 2023Review
- Article
- Determination of Secondary Structure of Proteins by Nanoinfrared Spectroscopy.Analytical chemistry · 2023Article
- Applications of Single-Molecule Vibrational Spectroscopic Techniques for the Structural Investigation of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2022Review
- Methodological advances and strategies for high resolution structure determination of cellular protein aggregates.The Journal of biological chemistry · 2022Review
- Nanoscale Infrared Spectroscopy Identifies Structural Heterogeneity in Individual Amyloid Fibrils and Prefibrillar Aggregates.The journal of physical chemistry. B · 2022Article
- Influence of Cortisol on the Fibril Formation Kinetics of Aβ42 Peptide: A Multi-Technical Approach.International journal of molecular sciences · 2022Article
- Contribution of Infrared Spectroscopy to the Understanding of Amyloid Protein Aggregation in Complex Systems.Frontiers in molecular biosciences · 2022Review
- Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods.Molecules (Basel, Switzerland) · 2020Review
- MIRRAGGE - Minimum Information Required for Reproducible AGGregation Experiments.Frontiers in molecular neuroscience · 2020Review
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibrils are composed of aggregated peptides or proteins in a fibrillar structure with a higher β-sheet content than in their native structure. To characterize them, we used an innovative tool that coupled infrared spectroscopy with atomic force microscopy (AFM-IR). With this method, we show that we can detect different individual aggregated species from oligomers to fibrils and study their morphologies by AFM and their secondary structures based on their IR spectra. AFM-IR overcomes the weak spatial resolution of usual infrared spectroscopy and achieves a resolution of ten nanometers, the size of isolated fibrils. We characterized oligomers, amyloid fibrils of Aβ42 and fibrils of α-synuclein. To our surprise, we figured out that the nature of some surfaces (ZnSe) used to study the samples induces destructuring of amyloid samples, leading to amorphous aggregates. We strongly suggest taking this into consideration in future experiments with amyloid fibrils. More importantly, we demonstrate the advantages of AFM-IR, with a high spatial resolution (≤ 10 nm) allowing spectrum recording on individual aggregated supramolecular entities selected thanks to the AFM images or on thin layers of proteins.
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