Investigation of α-synuclein and Amyloid-β(42)-E22 Δ oligomers using SiN nanopore functionalized with L-dopa.
Fiche publication
Date publication
août 2022
Journal
Chemistry, an Asian journal
Auteurs
Membres identifiés du Cancéropôle Est :
Dr PICAUD Fabien
Tous les auteurs :
Abrao-Nemeir I, Bentin J, Meyer N, Janot JM, Torrent J, Picaud F, Balme S
Lien Pubmed
Résumé
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 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-β and α-synuclein, two biomarkers of degenerative diseases. In the first application, we demonstrate that the α-synuclein WT is more prone to form dimers than the variant A53T. In the second one, we show for the Aβ(42)-E22Δ (Osaka mutant) that the addition of Aβ(42)-WT monomers increase the polymorphism of oligomers, while the incubation with Aβ(42)-WT fibrils generates larger aggregates.
Mots clés
Aggregation, amyloid-β, α-synuclein, nanopore, single molecule
Référence
Chem Asian J. 2022 08 29;: