What is PepLock?
PepLock is a family of short peptide anchors that give proteins, peptides, antibodies and enzymes built-in immobilisation on solid surfaces. It is a Biotome technology. The anchor can be built into a recombinant protein's sequence, included during solid-phase peptide synthesis, or attached chemically. A PepLock-tagged molecule then attaches to its intended surface in a single aqueous step, site-specifically and with consistent orientation, without coupling reagents, capture proteins or extra tags. In plain language, it is protein superglue.
Copy link to What is PepLock?Is PepLock a chemical linker or a conjugation reagent?
Not in the usual sense. PepLock is a short peptide anchor that becomes part of the molecule you want to immobilise. It can be encoded in a recombinant protein's sequence, included during solid-phase peptide synthesis, or attached chemically. Once the anchor is part of the molecule, attaching it to a surface needs no coupling reagents and no activation chemistry: the PepLock-tagged molecule attaches in a single aqueous step, site-specifically and with consistent orientation.
Copy link to Is PepLock a chemical linker or a conjugation reagent?How is PepLock introduced into a protein or peptide?
There are three routes. For recombinant proteins the anchor is built into the sequence and expressed with the rest of the protein. For synthetic peptides, it is included during solid-phase peptide synthesis. It can also be attached chemically. The existing expression and purification workflow is kept. Immobilisation becomes the last step of the workflow rather than a separate chemistry project. A PepLock-tagged molecule attaches to the intended surface in a single aqueous step.
Copy link to How is PepLock introduced into a protein or peptide?Does PepLock need a catalyst, a partner protein or a capture protein?
No. PepLock does not need a partner protein or catalyst. Once part of the molecule, a PepLock-tag attaches in a single aqueous step. There are no coupling reagents, no capture proteins such as streptavidin, and no extra tags. Attachment is site-specific, with consistent orientation.
Copy link to Does PepLock need a catalyst, a partner protein or a capture protein?How does PepLock differ from EDC/NHS coupling?
EDC/NHS coupling activates a carboxylated surface with reagents and then reacts it with amines on the protein. Any accessible lysine can take part, so the attachment point and orientation vary from molecule to molecule. PepLock needs no coupling reagents: the anchor is part of the molecule, attachment happens in a single aqueous step, and orientation is consistent. Biotome has compared PepLock head to head with EDC/NHS coupling on carboxylated microspheres; the results are in the data pack, available under NDA.
Copy link to How does PepLock differ from EDC/NHS coupling?How does PepLock differ from streptavidin-biotin?
Streptavidin-biotin immobilisation needs the molecule to be biotinylated and the surface to carry streptavidin, a capture protein, so every surface includes a second protein. Chemical biotinylation also labels whichever residues are accessible. PepLock removes both requirements. The anchor is part of the molecule, there is no capture protein on the surface, and a PepLock-tagged molecule attaches in a single aqueous step, site-specifically and with consistent orientation. Attachment withstands washes, detergents, salts, acids, bases and chaotropes.
Copy link to How does PepLock differ from streptavidin-biotin?How does PepLock differ from His-tag or Ni-NTA capture?
His-tag capture on Ni-NTA surfaces is designed to release the protein under imidazole, EDTA and other chelators, reducing agents or low pH. That suits purification, but not a surface that must hold a protein through repeated use or sample matrices containing those agents. Protein and metal can leach from the surface over time, and histidine-rich proteins can bind non-specifically. PepLock attachment withstands washes, detergents, salts, acids, bases and chaotropes. The two are complementary: PepLock is compatible with His6 tags, Ni-NTA purification and anti-His antibodies, so a protein can carry both and keep its existing purification workflow.
Copy link to How does PepLock differ from His-tag or Ni-NTA capture?How does PepLock differ from SpyTag/SpyCatcher and other isopeptide tag pairs?
SpyTag/SpyCatcher and other isopeptide tag pairs join a short peptide tag to a partner protein. To immobilise with them, the partner protein has to be produced, purified and placed on the surface first, and some pairs also rely on an added ligase. PepLock has no partner. A PepLock-tagged molecule attaches without a partner protein, in a single aqueous step, with no catalyst and no coupling reagents, and with consistent orientation.
Copy link to How does PepLock differ from SpyTag/SpyCatcher and other isopeptide tag pairs?What surfaces does PepLock bind?
PepLock attachment has been demonstrated on magnetic (carboxylated) beads, treated polystyrene plates and beads, nitrocellulose strips and membranes, polycarbonate and other functional plastics, gold microspheres and carbon-ink electrodes. Attachment occurs on the intended assay surface, whether that is a treated plate, a bead, nitrocellulose or another functional polymer. PepLock-tagged molecules do not appreciably bind untreated polypropylene, polyethylene or polystyrene labware.
Copy link to What surfaces does PepLock bind?Does PepLock stick to lab plastics?
No, not appreciably. PepLock-tagged molecules do not appreciably bind untreated polypropylene, polyethylene or polystyrene labware, so they handle like any other reagent through tubes, tips and storage plates. Attachment occurs on the intended assay surface, whether that is a treated plate, a bead, nitrocellulose or another functional polymer.
Copy link to Does PepLock stick to lab plastics?Does PepLock work with my existing purification tags?
Yes. PepLock is compatible with common purification tags and workflows, including His6 and FLAG tags, Ni-NTA, anti-His and anti-FLAG antibodies, and Protein A/G. The existing expression and purification workflow is kept. Immobilisation becomes the last step of the workflow rather than a separate chemistry project.
Copy link to Does PepLock work with my existing purification tags?What molecules has PepLock been demonstrated with?
PepLock has been demonstrated with eGFP, nanobodies (both VHH and VNAR), enzymes, human IgG, mouse IgG and synthetic peptides. It has been confirmed in ELISA, lateral flow, electrochemistry and flow cytometry. In peptide serology, PepLock-tagged peptides show robust binding and improved epitope presentation. PepLock is an early-stage technology. Applications beyond the confirmed formats are proposed, not yet validated.
Copy link to What molecules has PepLock been demonstrated with?What applications is PepLock aimed at?
Any application where a protein or peptide has to be attached to a surface robustly, in a known orientation, and stay there in use. PepLock has been demonstrated in diagnostics (ELISA, lateral flow, electrochemistry and flow cytometry) and with binders such as IgG and nanobodies. Beyond that, Biotome sees PepLock opening up immobilised enzymes and biocatalysis, durable surfaces in bioprocessing, and research tools from bead assays to arrays; the applications page sets out the wider field. PepLock is an early-stage technology. Applications beyond the confirmed formats are proposed, not yet validated.
Copy link to What applications is PepLock aimed at?Can PepLock-tagged molecules be coupled to particles?
Yes. PepLock attachment has been demonstrated on magnetic (carboxylated) beads, treated polystyrene plates and beads, and gold microspheres, and the data pack includes a head-to-head comparison against EDC/NHS coupling on carboxylated microspheres. A particle is a surface like any other: the tagged molecule attaches in one aqueous step, site-specifically and with consistent orientation, and the attachment withstands washes, detergents, salts, acids, bases and chaotropes. PepLock-tagged molecules do not appreciably bind untreated polypropylene, polyethylene or polystyrene labware.
Copy link to Can PepLock-tagged molecules be coupled to particles?What conditions does the attachment survive?
PepLock attachment withstands washes, detergents, salts, acids, bases and chaotropes. That matters wherever a surface is washed hard or kept in use: stringent assay washes, cleaning cycles, and flow reactors and process lines. The PepLock data pack is available under NDA, followed by a technical demonstration. Request it through the enquiry form or at peplock@biotome.com.au.
Copy link to What conditions does the attachment survive?Can I see the data?
Yes. The PepLock data pack is available under NDA, followed by a technical demonstration. It covers a head-to-head comparison against EDC/NHS coupling on carboxylated microspheres; coating titrations on nitrocellulose, polycarbonate and carbon electrode surfaces; nanobody and IgG binding and target capture on plates and beads; and peptide-epitope capture on microspheres and plates, including serum ELISA. Request it through the enquiry form or at peplock@biotome.com.au.
Copy link to Can I see the data?Who owns PepLock and what is the IP position?
PepLock is a Biotome technology, invented by Luke Marshall, Dr Samuel Lundin and Paige Bebee. Biotome Pty Ltd is based in Perth, Western Australia, at the Harry Perkins Institute of Medical Research. An international (PCT) patent application was filed in June 2026, and further filings are in progress. Biotome is speaking with licensing partners and investors.
Copy link to Who owns PepLock and what is the IP position?How do I license PepLock or invest in Biotome?
Start with a short conversation. Biotome is speaking with licensing partners and investors in PepLock. Use the enquiry form on the Work with us page or email peplock@biotome.com.au, and say whether your interest is licensing, collaboration or investment. The usual path is an enquiry, a call, an NDA, the data pack, a technical demonstration and then an evaluation in your own application.
Copy link to How do I license PepLock or invest in Biotome?