Characterization by Nano-Infrared Spectroscopy of Individual Aggregated Species of Amyloid Proteins
| Autor: | Vincent Raussens, Vincent Van Hemelryck, Alexandre Dazzi, Jean Marie Ruysschaert, Jehan Waeytens, Ariane Deniset-Besseau |
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| Rok vydání: | 2020 |
| Předmět: |
Amyloid
Materials science Spectrophotometry Infrared AFM-IR photothermal infrared nanospectroscopy Pharmaceutical Science Infrared spectroscopy macromolecular substances Microscopy Atomic Force Fibril Article Fluorescence Protein Structure Secondary Analytical Chemistry lcsh:QD241-441 amyloid fibrils 03 medical and health sciences lcsh:Organic chemistry Spectroscopy Fourier Transform Infrared mental disorders Drug Discovery Benzothiazoles oligomers Physical and Theoretical Chemistry Selenium Compounds 030304 developmental biology 0303 health sciences Amyloid beta-Peptides Thin layers aggregated species 030302 biochemistry & molecular biology Organic Chemistry Resolution (electron density) Sciences bio-médicales et agricoles Peptide Fragments Amorphous solid Characterization (materials science) Spectrometry Fluorescence Zinc Compounds Chemistry (miscellaneous) alpha-Synuclein Biophysics Molecular Medicine |
| Zdroj: | Molecules, Vol 25, Iss 2899, p 2899 (2020) Molecules Volume 25 Issue 12 Molecules, 25 (12 |
| ISSN: | 1420-3049 |
| DOI: | 10.3390/molecules25122899 |
| Popis: | Amyloid fibrils are composed of aggregated peptides or proteins in a fibrillar structure with a higher &beta 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 A&beta 42 and fibrils of &alpha 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 (&le 10 nm) allowing spectrum recording on individual aggregated supramolecular entities selected thanks to the AFM images or on thin layers of proteins. |
| Databáze: | OpenAIRE |
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