Portal Biotech
| Portal Biotech | |
|---|---|
 | |
| Type | Private |
| Industry | Proteomics, nanopore instruments |
| Founded | 2021 |
| Headquarters | London, England; laboratory work in Groningen, Netherlands |
| Products | Nanopore Peptide Sensing; full-length protein analysis (early access) |
| Website | portalbiotech.com |
Portal Biotech is a London company building nanopore instruments to read proteins. It was formed in 2021 as a spinout of the University of Groningen in the Netherlands, on the engineered protein pores of the laboratory of the chemist Giovanni Maglia, who co-founded it and is its chief scientific officer.[1][2] Its aim, in its own words, is to "see proteins as they really are", at full length and one molecule at a time. The method it uses is described in Nanopore protein sequencing.[3]
Problem
DNA is easy to push through a pore, because every base carries the same negative charge and an electric field pulls the whole strand along. Proteins have no such handle. In the words of one of the company's founders, "They're sometimes positive, sometimes negative, it's a real mixture."[a] A protein must also be unfolded before it fits, and the modifications that change what a protein does, such as an added phosphate group, are the features that existing methods most often miss. The same interview puts the gap in one line: "There is currently no fast, scalable way to fully sequence proteins."[1]
Technology
Maglia, who did postdoctoral work in Oxford on DNA nanopore sequencing, joined the University of Groningen in 2014.[2] The company says its technology "evolved from the pioneering work from the Maglia Lab".[3] Three papers from that laboratory show the steps.
In 2019 a group there engineered the diameter of the fragaceatoxin C (FraC) pore, a protein from a sea anemone, to take peptides of different lengths. The pores told apart two peptides that differed by a single amino acid, alanine against glutamate, and at pH 3.8 the depth of a current blockade tracked the mass of the peptide, with a resolution of 44 daltons.[4] In 2021 the laboratory built a 900 kDa machine from parts taken from all three domains of life: a nanopore linked to a mammalian proteasome activator, with an archaeal 20S proteasome set into it to unfold a protein and feed it through.[5] In 2024 it reported that a ring of charges spaced about 1 nm apart in the lumen of the CytK pore creates an electro-osmotic flow of about 20 pN at -100 mV, strong enough to carry unstructured natural polypeptides through the pore against the electric field.[6] That is about the force of the electric field on a strand of single-stranded DNA.
The company's interview describes adding an electro-osmotic approach so that proteins of mixed charge can be fed through the pore in a controlled way, with machine learning interpreting the signal.[1] It plans to move the pores onto a chip, to build a desktop instrument, and to sell sample-preparation kits and software with it.[1]
Products and status
The company's site lists Nanopore Peptide Sensing, for quantifying peptides and analyzing their modifications in a workflow described as compatible with mass spectrometry, and full-length protein analysis, which it says reads intact proteins end to end and locates modifications. It also lists benchtop instruments for academic, biopharmaceutical and industrial laboratories, protein characterization services run in its own laboratories, and an Early Access Programme open to commercial and academic groups.[3] The company is a major sponsor of the Proteoform Alliance, formerly the Consortium for Top-Down Proteomics.[3] The team works in the United Kingdom and the Netherlands.[2]
No instrument that sequences an unknown protein from end to end has been shown in the papers cited in Nanopore protein sequencing; the field's published results are fingerprinting, reading of modifications and the reading of known peptides.
At Molecular Reality
Molecular Reality Corporation lists the Maglia laboratory among the groups in its atlas of the field, The Hole World. The group at Groningen is one of the atlas's flagship entries, credited with 45 papers between 2012 and 2026 and drawn with a pore labelled "Fragaceatoxin C", with the note "Large engineered pores for proteins".[7]
See also
Notes
References
- ^ a b c d e "Bringing protein sequencing into the 21st century". Science Creates. Retrieved October 25, 2026.
- ^ a b c "Impact: nanopore technology for protein sequencing and personalized healthcare". University of Groningen. May 19, 2026.
- ^ a b c d "Portal Biotech". Portal Biotech. Retrieved October 25, 2026.
- ^ Huang, G.; Voet, A.; Maglia, G. (2019). "FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution". Nature Communications 10: 835. doi:10.1038/s41467-019-08761-6.
- ^ Zhang, S. et al. (2021). "Bottom-up fabrication of a proteasome-nanopore that unravels and processes single proteins". Nature Chemistry 13 (12): 1192-1199. doi:10.1038/s41557-021-00824-w.
- ^ Sauciuc, A. et al. (2024). "Translocation of linearized full-length proteins through an engineered nanopore under opposing electrophoretic force". Nature Biotechnology 42 (8): 1275-1281. doi:10.1038/s41587-023-01954-x.
- ^ "The Hole World". Molecular Reality Corporation. September 26, 2026.