Biopharmaceutical R&D

Finding the hits conventional screening misses

Chemtelliq screens a DNA-encoded library of 343 million synthesised compounds, identifies the genuine hits with its own AI models, and optimises them through structure-based design and bench validation.

Structure-based design A docked binder in the target pocket — the picture our chemists optimise against, round by round.
What we do

Three business areas

One discovery engine feeding two development modalities.

Three stages side by side. DNA-encoded library: small molecules
                      each attached to a DNA double helix that encodes their structure.
                      Selection against target protein: the library is washed over an
                      immobilised target; one compound stays bound while the rest leave
                      in the wash fraction. Decoding: the bound compounds' DNA tags are
                      amplified by PCR, read by high-throughput sequencing, and the hit
                      is resynthesised without its tag for validation.
01 — Hit discovery

DNA-encoded library

Every compound carries a DNA barcode recording how it was made. That lets 343 million of them meet a target in a single tube: what binds is kept, what does not is washed away, and sequencing reads back the answer.

A peptide-drug conjugate broken into three parts: a chain of linked
                      beads labelled Peptide, a coiled Linker, and a filled circle
                      labelled Payload. Below, each part is expanded. Homing peptides:
                      target specific, cell penetrating, non-cell penetrating. Linkers:
                      non-cleavable, cleavable, stimuli responsive to pH, GSH or enzymes.
                      Payloads: cytotoxic drugs, radionuclides, imaging agents.
02 — Development

Peptide-drug conjugates

The peptide finds the receptor, the linker holds the payload until it should not, and the payload does the work. Each of the three is a design choice in its own right — how the peptide enters the cell, whether the linker releases on pH, glutathione or an enzyme, and whether the payload kills, irradiates or images.

Two approaches side by side. PROTAC: a bifunctional molecule brings
                      an E3 ligase and the target protein together, the target is
                      ubiquitinated and destroyed by the proteasome, and the molecule is
                      released and reused. RIPTAC: a linker holds a tumour-specific
                      protein against an essential protein; in a normal cell the
                      tumour-specific protein is absent so nothing happens, while in a
                      tumour cell the complex forms and the essential protein's function
                      is abrogated by induced proximity, without degradation.
03 — Development

Targeted protein degradation

A degrader recruits the cell’s own disposal machinery to remove a protein rather than block it — and is released to do it again. Induced proximity can also disable a protein outright, acting only where the tumour-specific partner exists.

How we work

Prediction and experiment, one team

Physical chemistry, machine learning and bench work sit on the same clock. That loop is the platform.

In silico

Structure & docking

Our physical chemists model protein structures and predict molecular docking to explain how a hit binds — then modify it, round by round, through lead optimisation.

In silico

AI hit identification

Machine learning and deep learning models read the selection data from a 343-million-compound library and separate genuine binders from artefacts — the step that decides what is worth making.

At the bench

Wet-lab execution

Protein production, binding characterisation and cell-based validation are run by our own team. Results come back in days, and every result — including the negatives — retrains the model.

Looking for a discovery partner?

We collaborate with pharmaceutical companies, academic groups and investors on targets that conventional screening has struggled with.