Aβ42 fibril and non-fibril oligomers characterization using a nanopipette

Imad Abrao-Nemeir; Nathan Meyer; Alexis Nouvel; Saly Charles-Achille; Jean-Marc Janot; Joan Torrent; Sebastien Balme

doi:10.1016/j.bpc.2023.107076

Aβ42 fibril and non-fibril oligomers characterization using a nanopipette

Biophys Chem. 2023 Sep:300:107076. doi: 10.1016/j.bpc.2023.107076. Epub 2023 Jul 17.

Authors

Imad Abrao-Nemeir¹, Nathan Meyer², Alexis Nouvel¹, Saly Charles-Achille¹, Jean-Marc Janot¹, Joan Torrent³, Sebastien Balme⁴

Affiliations

¹ Institut Européen des Membranes, UMR5635 University of Montpellier ENCSM CNRS, Place Eugène Bataillon, 34095 Montpellier Cedex 5, France.
² Institut Européen des Membranes, UMR5635 University of Montpellier ENCSM CNRS, Place Eugène Bataillon, 34095 Montpellier Cedex 5, France; INM, University of Montpellier, INSERM, Montpellier, France.
³ INM, University of Montpellier, INSERM, Montpellier, France.
⁴ Institut Européen des Membranes, UMR5635 University of Montpellier ENCSM CNRS, Place Eugène Bataillon, 34095 Montpellier Cedex 5, France. Electronic address: sebastien.balme@umontpellier.fr.

PMID: 37480837
DOI: 10.1016/j.bpc.2023.107076

Abstract

The Aβ42 aggregates with different structures and morphology was investigated through a single molecule label-free technique. To this end, the quartz nanopipettes were functionalized with polyethylene glycol. The set of Aβ42- epigallocatechin-3-gallate fibrils with length (from 85 nm to 250 nm) obtained by sonication was detected. The comparison of experimental and computed value of the amplitude of relative current blockade using a geometrical model show that for fibrils longer than 80 nm, the discriminating parameter is their diameter. Then, non-fibril oligomers obtain from Aβ42(Osaka) aggregation at different time seed was investigated. The analysis of the amplitude of relative current blockade shows that detected oligomers are smaller than 30 nm regardless the aggregation time. In addition, the wide distributions of the dwell time suggests the polymorph character of the sample.

Keywords: Amyloids; Nanopore; Single molecule.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Alzheimer Disease*
Amyloid / chemistry
Amyloid beta-Peptides* / chemistry
Humans
Peptide Fragments / chemistry

Substances

amyloid beta-protein (1-42)
Amyloid beta-Peptides
Peptide Fragments
Amyloid