Work

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

Year: 2026

Type: preprint

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.

Source: bioRxiv (Cold Spring Harbor Laboratory)

DOI: 10.64898/2026.01.08.698148

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

Institutions: University of Groningen, Zernike Institute for Advanced Materials, ETH Zurich, Laboratory of Organic Chemistry

Language: English

Topic: Nanopore and Nanochannel Transport Studies

Subfield: Biomedical Engineering

Field: Engineering

Domain: Physical Sciences

Open Access status: green

OpenAlex ID: W7119480106

Cites: 20

Cited by: 3

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