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A January 2026 preprint reports a nanopore method that combines an unfoldase enzyme with enhanced electroosmotic flow to identify proteins during a single pass through a pore. The authors also report signal differences associated with single-amino-acid substitutions. That is a step toward protein sequencing, not evidence that nanopores can yet routinely read arbitrary proteins de novo.
What the January 2026 preprint reports
In a preprint posted on 8 January 2026, Bonini and colleagues describe using an unfoldase and a nanopore with enhanced electroosmotic flow to identify proteins continuously during single nanopore passes. The authors write: “By using an unfoldase and a nanopore with enhanced electroosmotic flow, here we show the continuous identification of generic proteins during single nanopore passes.” The abstract also reports differences in signals associated with single-amino-acid substitutions, interpreted against reference signals. Read the authors’ bioRxiv preprint or its University of Groningen research record.
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The title describes identification of full-length proteins, but the reported result should be read as identification and sequence-relevant discrimination—not as a general method that reconstructs the complete amino-acid sequence of any protein. “Single-amino-acid resolution” here refers to reported signal differences associated with substitutions; it is not a quoted accuracy rate or a guarantee that every residue can be called correctly.
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How an unfoldase and electroosmotic flow help
A nanopore detects changes in ionic current as molecules move through a tiny pore. For proteins, interpreting those changes is difficult: amino acids differ chemically and in charge, proteins can fold into complex shapes, and their movement must be controlled closely enough for signal features to be useful.
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The reported approach combines two elements. An unfoldase is an enzyme that helps unfold proteins, while enhanced electroosmotic flow provides a way to drive or maintain movement through the pore. In broad terms, motor enzymes can slow passage and give a sensor more time to register current changes; electroosmotic force can help thread proteins when their charge makes electrophoretic movement difficult. The study abstract establishes that the team combined these elements, but does not provide enough detail to assert a more specific mechanism for this experiment.
Protein identification is not the same as de novo sequencing
| Question | What this preprint supports | What it does not establish |
|---|---|---|
| Can the method identify proteins in a nanopore pass? | The authors report continuous identification of generic proteins during single passes. Source: bioRxiv preprint. | The abstract does not establish broad coverage across arbitrary proteins or routine performance on real-world samples. |
| Can it distinguish a one-amino-acid change? | The authors report signal differences associated with single-amino-acid substitutions relative to reference signals. Source: bioRxiv preprint. | It does not provide a general residue-calling accuracy, error rate, or proof that a full sequence can be recovered without a reference. |
| Does it demonstrate de novo sequencing? | The authors present the work as progress toward protein sequencing and high-throughput proteomics. | The abstract does not show routine reconstruction of complete, previously unknown protein sequences. A 2025 review distinguishes advances in protein identification from the still-open challenge of de novo sequencing. Read the review in Trends in Biochemical Sciences. |
| Can its performance be compared numerically with alternatives? | The abstract supports the combination of an unfoldase and enhanced electroosmotic flow. | No suitable throughput, speed, accuracy, protein-coverage, or sample-count statistic is established in the available abstract or institutional record. The records also do not establish superiority over other approaches. |
This distinction matters because a reference-based identification or fingerprinting task can ask whether a measured signal matches known proteins or variants. De novo sequencing would require recovering the amino-acid order without relying on a known reference. The reported signal discrimination is relevant to sequencing, but it does not by itself establish that broader capability.
Independent reader supportYour contribution helps us test, update, and keep practical guides available for everyone.What remains difficult for nanopore protein reading
A 2025 review describes motor-assisted translocation and electroosmotic-force-driven threading as promising directions, while identifying unresolved technical constraints. Enzyme motion can be irregular; some systems require special tags; and analyzing naturally occurring proteins remains difficult. These challenges affect whether a signal can be controlled and interpreted consistently, not just whether a protein can be made to pass through a pore. Read the 2025 review on single-molecule protein sequencing with nanopores.
The abstract available for this preprint does not supply numeric performance results that would answer how quickly the method works, what fraction of proteins it can identify, or how often it calls a substitution correctly. Those measures should not be inferred from the phrase “single-amino-acid resolution.”
Peer-review status and commercial context
The work was posted as a preprint. The PubMed Central record labels it a preprint and states that it has not yet been peer reviewed. The records available through 7 October 2026 do not establish whether a journal version appeared afterward, so it should be cited as a preprint rather than as peer-reviewed journal research unless a later publication record is confirmed. Check the PubMed Central record.
The author affiliations include Portal Biotech. The preprint discloses that Giovanni Maglia and Andrew Heron are founders, directors, and shareholders of Portal Biotech Limited, which is described as working on nanopore technology. That connection is relevant context when assessing a promising result; it does not invalidate the findings, nor does it establish that a commercial protein-sequencing product is available.
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