Single-molecule identification of full-length proteins with single-amino-acid resolution using nanopores

bioRxiv (Cold Spring Harbor Laboratory) 2026 Preprint Open access

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Authors: Andrea Bonini, Chunzhe Lu, Luca Mantovanelli, Roderick Corstiaan Abraham Versloot, Alwin Jansen, Peter O Connell Stack, Vasiliki Tsousi, Pascal Knecht, Kathrin Lang, Andrew Heron, Giovanni Maglia
DOI: 10.64898/2026.01.08.698148
Cited by: 2
References: 20

Abstract

Nanopore-based technologies show promise in single-molecule protein sequencing. By using an unfoldase and a nanopore with enhanced electroosmotic flow, here we show the continuous identification of generic proteins during single nanopore passes. This approach enables the recording of differences in charge and size from single amino acid substitutions compared to reference signals, paving the way for single-molecule protein sequencing and high-throughput proteomics.

Fields of Study & Subjects

Nanopore and Nanochannel Transport Studies Membrane-based Ion Separation Techniques Ion-surface interactions and analysis

Publication details

Journal / source
bioRxiv (Cold Spring Harbor Laboratory)
Publisher
openRxiv
Publication date
8 January 2026
Language
EN
Document type
Preprint