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Proceedings Paper

Structure of toxic oligomers from Ab1-42 peptide probed at the nanometer scale by TERS and NanoIR and interaction with membrane (Conference Presentation)
Author(s): Sébastien Bonhommeau; Sarah Henry; David Talaga; Christophe Cullin; Michael Molinari; Sophie Lecomte

Paper Abstract

The toxicity of amyloids is a subject under intense scrutiny. Many studies link this toxicity to the existence of various intermediate structures prior to the fiber formation and/or their specific interaction with membranes. For the first time, natural Ab1–42 fibrils (WT) implicated in Alzheimers disease, as well as highly toxic oligomers (oG37C), are chemically characterized at the scale of a single structure by Tip-Enhanced Raman Spectroscopy and NanoIR. TERS is a powerful technique combining the high sensitivity of surface-enhanced Raman scattering (SERS) and the nanoscale lateral spatial resolution of atomic force microscopy (AFM). A careful examination of amide I and amide III bands allows us to clearly distinguish WT fibers organized in parallel b-sheets from the small and more toxic oG37C oligomers organized in anti-parallel b-sheets. The interaction between membrane models and Aβ1−42 peptides and variants were also investigated using various biophysical techniques and NanoIR spectroscopy. We established that toxic stable oligomeric form (oG37C) interacts strongly with membranes leading to its disruption.

Paper Details

Date Published: 17 September 2018
Proc. SPIE 10726, Nanoimaging and Nanospectroscopy VI, 107260X (17 September 2018); doi: 10.1117/12.2319947
Show Author Affiliations
Sébastien Bonhommeau, Univ. de Bordeaux (France)
Sarah Henry, Institut de Chimie et de Biologie des Membranes et des Nanoobjects (France)
David Talaga, Institut des Sciences Moléculaires (France)
Christophe Cullin, Institut de Chimie et de Biologie des Membranes et des Nanoobjects (France)
Michael Molinari, Lab. de Microscopies et d'Etudes des Nanostructures (France)
Sophie Lecomte, Ctr. National de la Recherche Scientifique (France)

Published in SPIE Proceedings Vol. 10726:
Nanoimaging and Nanospectroscopy VI
Prabhat Verma; Alexander Egner, Editor(s)

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