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PepLock, built-in immobilisation

Technology

Immobilisation as a property of the molecule

PepLock is a family of short peptide anchors that give proteins, peptides, antibodies and enzymes built-in immobilisation on solid surfaces. Think of it as protein superglue.

How it works

From sequence to surface in four steps

A long translucent molecular chain winding through the dark, with one short segment glowing mint green.
The PepLock anchor is encoded as part of the molecule itself. Illustration.

01 · Encode

The anchor is part of the molecule

The anchor can be built into a recombinant protein's sequence, included during solid-phase peptide synthesis, or attached chemically. There are many flavours of PepLock for different applications.

Green proteins drifting away from a cell surface, each trailing a short glowing tether.
Expression and purification proceed as usual; the tag travels with the protein. Illustration.

02 · Express and purify

Your workflow stays the same

The existing expression and purification workflow is kept. Compatible with common purification tags and workflows: His6, FLAG, Ni-NTA, anti-His, anti-FLAG, Protein A/G.

Inside a clear droplet on a dark surface, three green proteins stand on glowing tethers while two more descend, tether first.
A PepLock-tagged protein attaches in a single aqueous step. Illustration.

03 · Immobilise

One aqueous step onto the surface

Attaches in a single aqueous step. No coupling reagents, no capture proteins, no extra tags. Site-specific attachment with consistent orientation.

A field of upright green proteins on glowing tethers inside an off-white plate well, several with a small blue molecule docked on top.
Attached with consistent orientation, so the working face stays available. Illustration.

04 · Perform

Oriented and working on the surface

Higher loading and preserved function compared with conventional immobilisation. Attachment withstands washes, detergents, salts, acids, bases and chaotropes. Confirmed in ELISA, lateral flow, electrochemistry and flow cytometry.

Conventional immobilisation

What conventional immobilisation costs you

For each method: what it requires, and where orientation, retention or simplicity is lost.

Conventional immobilisation methods compared with PepLock
MethodWhat it requiresWhere it losesWith PepLock
Passive adsorptionA suitable surface and an incubation step; the protein sticks through nonspecific contacts with the surface.Orientation is random, some molecules partly unfold or present their binding sites to the surface, and adsorbed protein can be lost in washes and detergents.The attachment point is built into the molecule. Orientation is consistent. Attachment withstands washes, detergents, salts, acids, bases and chaotropes.
EDC/NHS couplingActivation of a carboxylated surface with coupling reagents, then reaction with amines on the protein, with buffer changes and a quench step.Any accessible lysine can react, so the attachment point and orientation vary between molecules, and binding sites can be modified or blocked.No coupling reagent and no activation step: a PepLock-tagged molecule attaches in one aqueous step, site-specifically and with consistent orientation.
Maleimide and NHS-ester chemistryCrosslinking reagents that target cysteines or amines, often with a reduction or activation step and removal of excess reagent.Site control depends on engineering a unique site; otherwise attachment spreads across many residues, and the reagents are sensitive to hydrolysis.Surface attachment needs no crosslinker: the anchor is built into the sequence, added during synthesis, or attached chemically. Attachment is a single aqueous step with consistent orientation.
Streptavidin-biotinBiotinylation of the molecule and a surface coated with streptavidin, a capture protein.Every surface carries a second protein, adding cost and another component to qualify, and chemical biotinylation is not site-specific.No capture protein and no biotinylation step: a PepLock-tagged molecule attaches without a capture protein, site-specifically, in one aqueous step.
His-tag / Ni-NTA captureA polyhistidine tag on the protein and a nickel-chelate surface.Capture is designed to release under imidazole, EDTA and other chelators, reducing agents or low pH, which 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.Attachment withstands washes, detergents, salts, acids, bases and chaotropes; PepLock is compatible with a His6 tag kept for purification.
SpyTag/SpyCatcher and other isopeptide tag pairsA peptide tag on the molecule and its partner protein, produced, purified and placed on the surface first; some pairs also rely on an added ligase.The partner protein adds a protein layer, its production and its cost to every surface.No partner protein and no catalyst: a PepLock-tagged molecule attaches in one aqueous step, with consistent orientation.

Scroll the table sideways to see every column.

With PepLock

What changes with PepLock

  • Attachment point

    Site-specific attachment with consistent orientation.

  • Loading and function

    Higher loading and preserved function compared with conventional immobilisation.

  • One step

    Attaches in a single aqueous step.

  • No added reagents

    No coupling reagents, no capture proteins, no extra tags.

  • No partner protein or catalyst

    PepLock needs no partner protein and no catalyst.

Durability and materials

Attachment that holds

Attachment withstands washes, detergents, salts, acids, bases and chaotropes.

Surfaces demonstrated

  • Magnetic (carboxylated) beads
  • Treated polystyrene plates and beads
  • Nitrocellulose strips and membranes
  • Polycarbonate and other functional plastics
  • Gold microspheres
  • Carbon-ink electrodes
Six PepLock-tagged green proteins standing on bead-chain tethers, one on each of six surfaces in a row: dark beads, pale beads, a clear multi-well plastic, a clear plastic slab, a gold slab and a porous carbon slab.
Illustration: one PepLock-tagged protein on each demonstrated surface type.

Handling

Handles like any other reagent

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.

Compatible with common purification tags and workflows:

  • His6
  • FLAG
  • Ni-NTA
  • anti-His
  • anti-FLAG
  • Protein A/G

Evidence

What the evidence covers

What the data pack contains

  • 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.
  • Peptide-epitope capture on microspheres and plates, including serum ELISA.

Available under NDA, followed by a technical demonstration.

Where each result stands

Confirmed
Confirmed in ELISA, lateral flow, electrochemistry and flow cytometry.
Demonstrated with
eGFP, nanobodies (VHH and VNAR), enzymes, human IgG, mouse IgG and synthetic peptides.
Proposed
PepLock is an early-stage technology. Applications beyond the confirmed formats are proposed, not yet validated.

Demonstrated with eGFP, nanobodies (VHH and VNAR), enzymes, human IgG, mouse IgG and synthetic peptides. In peptide serology, PepLock-tagged peptides show robust binding and improved epitope presentation.

See the data behind each step

We are speaking with licensing partners and investors.

Or email peplock@biotome.com.au