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

Autor: Imad Abrao‐Nemeir, Jeremy Bentin, Nathan Meyer, Jean‐Marc Janot, Joan Torrent, Fabien Picaud, Sebastien Balme
Rok vydání: 2022
Předmět:
Zdroj: Chemistry – An Asian Journal. 17
ISSN: 1861-471X
1861-4728
Popis: 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-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 increases the polymorphism of oligomers, while the incubation with Aβ(42)-WT fibrils generates larger aggregates.
Databáze: OpenAIRE
Externí odkaz: