Single-molecule identification of full-length proteins with single-amino-acid resolution using nanopores
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.
Authors
- Luca Mantovanelli (ORCID: https://orcid.org/0000-0001-9826-3869)
- Giovanni Maglia (ORCID: https://orcid.org/0000-0003-2784-0811)
- A. M. Jansen
- Roderick Corstiaan Abraham Versloot (ORCID: https://orcid.org/0000-0001-6407-9473)
- Andrea Bonini (ORCID: https://orcid.org/0009-0001-3550-3519)
- Pascal Knecht
- Peter O Connell Stack
- Chunzhe Lu
- Kathrin Lang
- Vasiliki Tsousi
- Andrew Heron
Institutions
- University of Groningen (NL)
- Department of Space (IN)
- ETH Zurich (CH)
Publication Details
- Journal
- bioRxiv (Cold Spring Harbor Laboratory)
- Published
- 2026-01-08
- DOI
- https://doi.org/10.64898/2026.01.08.698148
- Primary Topic
- Nanopore and Nanochannel Transport Studies
- Type
- article
- Field-Weighted Citation Impact
- 0.00