ArticleNature communications2026
Nanopore-based massively parallel sensing for peptide profiling and protein 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 2 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed.
- Probing Voltage Dependence Interaction of Cationic Peptides with Bacterial Porins at A Single-Molecule Level.Cell biochemistry and biophysics · 2026Article
- Review
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Authors and funding
29 authors.
Funding
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Abstract
Nanopore-based single-molecule sensing holds immense promise for revolutionizing proteomics, however, its practical application remains constrained by low throughput, suboptimal library preparation, and limited analytical power for complex, stochastic signals. To overcome these challenges, we develop a high-throughput nanopore sensing platform that couples a streamlined peptide library preparation strategy with an AI-driven analytical workflow, enabling accurate peptide differentiation and protein identification. Our analytical framework captures the distinct statistical signatures of peptides within massive single-molecule event streams, transforming them into reliable, information-rich fingerprints to achieve remarkable classification accuracy. We also apply this platform to establish a rapid and cost-effective workflow for antibody validation, facilitating precise epitope screening and semi-quantitative affinity determination. Critically, in a blinded study, this high-throughput sensing system demonstrates its robustness by unambiguously identifying multiple proteins from their complex enzymatic digests. By establishing an end-to-end pipeline from native proteins/peptides modification, parallel sensing to their identification, this work develops a scalable and powerful method for proteomics research.
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Registered trials
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