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Probing Amyloid Fibrils Secondary Structures by Infrared Nanospectroscopy: Experimental and Theoretical Considerations

Abstract

Amyloid fibrils are composed of aggregated peptides or proteins in a fibrillary structure with a higher β-sheet content than their native structure. Attenuated total reflection Fourier transform infrared spectroscopy only provides bulk analysis of a sample therefore it is impossible to discriminate between different aggregated structures. To overcome this limitation, near-field techniques like AFM-IR have emerged in the last twenty years to allow infrared nanospectroscopy. This technique obtains IR spectra with a spatial resolution of ten nanometres, the size of isolated fibrils. Here, we present essential practical considerations to avoid misinterpretations and artefacts during these analyses. Effects of polarization of the incident IR laser, illumination configuration and coating of the AFM probes are discussed, including the advantages and drawbacks of their use. This approach will improve interpretation of AFM-IR spectra especially for secondary structures determination of species not accessible using classical ATR-FTIR.

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Supplementary files

Article information


Submitted
03 Aug 2020
Accepted
04 Oct 2020
First published
05 Oct 2020

Analyst, 2020, Accepted Manuscript
Article type
Paper

Probing Amyloid Fibrils Secondary Structures by Infrared Nanospectroscopy: Experimental and Theoretical Considerations

J. Waeytens, J. Mathurin, A. Deniset, V. arluison, L. Bousset, H. Rezaei, V. Raussens and A. dazzi, Analyst, 2020, Accepted Manuscript , DOI: 10.1039/D0AN01545H

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