ArticleNature communications2026
Exopeptidase-assisted nanopore peptide sequence identification.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Exopeptidase-assisted nanopore peptide sequence identification.Nature communications · 2026Article
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Authors and funding
9 authors.
Funding
Abstract
Despite substantial progress in nanopore sensing, residue-by-residue peptide sequencing remains a major challenge. Herein, we present EANPSeq, an exopeptidase-assisted nanopore peptide identification strategy based on peptide libraries to decode the peptide sequence. By continuously recognizing the resulting fragments from digesting peptides stepwise through a nanopore, this approach could achieve the identification of peptide sequence based on the comparison of fragment data with libraries of shortened and mutated peptides, with the assistance of machine learning. Notably, compared with previously reported nanopore peptide sensing strategies, EANPSeq shows sufficient resolution to recognize the continuous sequence of peptides containing adjacent identical residues and to precisely localize post-translational modification (PTM) sites within consecutive residues. These proof-of-concept results highlight our nanopore-based strategy as a new avenue for single-molecule protein sequencing.
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Registered trials
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