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What did the researchers report?
In a preprint posted on 8 January 2026, Bonini and colleagues describe combining an unfoldase with a nanopore that has enhanced electroosmotic flow. The authors say the approach enabled continuous identification of generic proteins during single nanopore passes. They also report signal differences associated with single-amino-acid substitutions, comparing those signals with references. The preprint abstract and the University of Groningen record support those findings.
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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.” This is the authors’ description of their result, not a demonstration that the method can recover the complete sequence of any protein without a reference.
How does the enzyme help a nanopore read proteins?
A nanopore detects changes in ionic current as molecules pass through its tiny opening. Interpreting a protein’s signal is difficult: proteins can carry different charges, fold into complex shapes, and contain amino acids with distinct chemical properties. Their movement through the pore must also be controlled closely enough for current changes to be useful.
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In the reported approach, an unfoldase is paired with enhanced electroosmotic flow. The preprint establishes this combination and reports its identification result, but its abstract does not provide enough detail to support a more specific account of the enzyme’s mechanical action in this system.
More broadly, motor enzymes can slow a molecule’s movement to give a sensor more time to register signal features, while electroosmotic flow can help transport proteins when their charge makes electrophoretic movement difficult. These are active research strategies, not a settled, standard solution. A 2025 review describes motor-assisted translocation and electroosmotic-force-driven threading as a promising combination while noting unresolved problems, including irregular enzyme steps, special-tag requirements in some systems, and difficulties working with naturally occurring proteins. See the review, “Single-molecule protein sequencing with nanopores”.
Does single-amino-acid resolution mean the protein was sequenced?
Not necessarily. The preprint reports distinguishing signal differences associated with single-amino-acid substitutions against reference signals. That is sequence-relevant discrimination: it suggests the signal can reflect a change at one amino-acid position. It is not the same claim as reading an unknown protein’s entire amino-acid sequence from scratch.
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Clear out junk files and repair common Windows errorsFree Scan →Fix the driver behind crashes, sound loss and screen glitchesFind Drivers →Protein identification or fingerprinting can use observed signals to distinguish proteins or compare them with known references. De novo sequencing requires deriving the sequence without relying on a known reference. The preprint’s abstract supports the former and progress toward the latter; it does not establish routine, general de novo protein sequencing. A 2025 review likewise describes the distinction between protein identification advances and the still-open challenge of de novo sequencing: “Advancing nanopore technology toward protein identification and sequencing.”
Independent reader supportYour contribution helps us test, update, and keep practical guides available for everyone.What does the evidence not establish?
The abstract and institutional record do not provide a basis for quoting a numerical accuracy, error rate, throughput, sample count, or protein-coverage figure for this study. “Single-amino-acid resolution” should not be converted into any of those performance claims. Nor do the records establish comparative superiority over other nanopore protein methods across full-length native proteins, engineered constructs or fragments, enzyme-controlled or enzyme-free transport, tag requirements, or reproducibility.
The manuscript is a preprint. The PubMed Central record states that it has not yet been peer reviewed. The records cited here do not establish whether it was subsequently published in a journal, so its findings should be attributed to the authors as preprint results rather than presented as peer-reviewed conclusions.
Who is behind the work, and is there a product to use?
The author team includes researchers affiliated with the University of Groningen and Portal Biotech. The preprint discloses that Giovanni Maglia and Andrew Heron are founders, directors, and shareholders of Portal Biotech Limited, which it describes as engaged in nanopore technology development. That connection is relevant context when considering possible commercial development; it does not establish that the reported method is available as a product.
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1Repair Windows errors before they cause bigger problems2Scan for outdated or missing drivers - takes under a minute3Clear out junk files and repair common Windows errorsThe cited records describe laboratory research, not a commercially available protein-sequencing system or a service readers can access. The study therefore does not show that nanopore protein sequencing is ready for routine use in a lab, clinic, or consumer setting.
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