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.
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