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Analysis of Bacterial Amyloid Interaction with Lipidic Membrane by Orientated Circular Dichroism and Infrared Spectroscopies

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Bacterial Amyloids

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2538))

Abstract

Fourier transform infrared spectroscopy (FTIR), circular dichroism (CD), and orientated circular dichroism (OCD) are complementary spectroscopies widely used for the analysis of protein samples such as the amyloids commonly renowned as neurodegenerative agents. Determining the secondary structure content of proteins, such as aggregated β-sheets inside the amyloids and in various environments, including membranes and lipids, has made these techniques very valuable and complemental to high-resolution techniques such as nuclear magnetic resonance (NMR), X-ray crystallography, and cryo-electron microscopy. FTIR and CD are extremely sensitive to structural changes of proteins due to environmental changes. Furthermore, FTIR provides information on lipid modifications upon protein binding, whereas synchrotron radiation CD (SRCD) and OCD are sensitive to the subtle structural changes occurring in β-sheet-rich proteins and their orientation or alignment with lipid bilayers. FTIR and CD techniques allow the identification of parallel and antiparallel β-sheet content and are therefore complementary. In this chapter, we present FTIR and CD/OCD applications to study the interactions of bacterial amyloids with membranes and lipids. Moreover, we show how to decipher the spectroscopic signals to obtain information on the molecular structure of amyloids and their interaction with lipids, addressing potential amyloid insertion into membranes and the lipid bilayer adjustments observed.

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Acknowledgments

This work was supported by CNRS, CEA, Synchrotron SOLEIL, ULB and by a public grant overseen by the French National Research Agency (ANR) as part of the « Investissements d’Avenir » program through the “ADI 2021” project funded by the IDEX Paris-Saclay, ANR-11-IDEX-0003-02 (FT). This study contributes to the IdEx Université de Paris ANR-18-IDEX-0001.

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Authors and Affiliations

  1. Centre de Biologie structurale et de Bioinformatique, Structure et Fonction des Membranes Biologiques, Université libre de Bruxelles, Bruxelles, Belgium

    Jehan Waeytens & Vincent Raussens

  2. Institut de Chimie Physique, CNRS UMR8000, Université Paris-Sud, Université Paris-Saclay, Orsay, France

    Jehan Waeytens

  3. Laboratoire Léon Brillouin LLB, CEA, CNRS UMR12, Université Paris Saclay, Gif-sur-Yvette, France

    Florian Turbant & Véronique Arluison

  4. Université de Paris Cité, Paris, France

    Véronique Arluison

  5. Synchrotron SOLEIL, L’Orme des Merisiers, Gif-sur-Yvette, France

    Frank Wien

Authors
  1. Jehan Waeytens
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  2. Florian Turbant
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  3. Véronique Arluison
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  4. Vincent Raussens
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  5. Frank Wien
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Corresponding authors

Correspondence to Vincent Raussens or Frank Wien .

Editor information

Editors and Affiliations

  1. CEA Saclay, Lab Léon Brillouin UMR12 CEA/CNRS, Gif sur Yvette Cedex, France

    Véronique Arluison

  2. Synchrotron SOLEIL, Gif-sur-Yvette Cedex, France

    Frank Wien

  3. Departamento de Biología, University of Chile, Santiago, Chile

    Andrés Marcoleta

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© 2022 The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature

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Waeytens, J., Turbant, F., Arluison, V., Raussens, V., Wien, F. (2022). Analysis of Bacterial Amyloid Interaction with Lipidic Membrane by Orientated Circular Dichroism and Infrared Spectroscopies. In: Arluison, V., Wien, F., Marcoleta, A. (eds) Bacterial Amyloids. Methods in Molecular Biology, vol 2538. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2529-3_15

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  • DOI: https://doi.org/10.1007/978-1-0716-2529-3_15

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-2528-6

  • Online ISBN: 978-1-0716-2529-3

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