2022 · CHEMISTRY-AN ASIAN JOURNAL

Investigation of α-Synuclein and Amyloid-β(42)-E22Δ Oligomers Using SiN Nanopore Functionalized with L-Dopa

Abrao-Nemeir, Imad, Bentin, Jeremy, Meyer, Nathan, Janot, Jean-Marc, Torrent, Joan, Picaud, Fabien, Balme, Sebastien

Journal
CHEMISTRY-AN ASIAN JOURNAL
Année
2022
Volume
17
Numéro
20
Article
e202200726
Mois
OCT 17
DOI
10.1002/asia.202200726

Abstract

Solid-state nanopores are an emerging technology used as a high-throughput, label-free analytical method for the characterization of protein aggregation in an aqueous solution. In this work, we used Levodopamine to coat a silicon nitride nanopore surface that was fabricated through a dielectric breakdown in order to reduce the unspecific adsorption. The coating of inner nanopore wall by investigation of the translocation of heparin. The functionalized nanopore was used to investigate the aggregation of amyloid-beta and alpha-synuclein, two biomarkers of degenerative diseases. In the first application, we demonstrate that the alpha-synuclein WT is more prone to form dimers than the variant A53T. In the second one, we show for the A beta(42)-E22 Delta (Osaka mutant) that the addition of A beta(42)-WT monomers increases the polymorphism of oligomers, while the incubation with A beta(42)-WT fibrils generates larger aggregates.

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