NAMED CAPABILITY · ANTIBODY AND PROTEIN ENGINEERING
NAMED CAPABILITY
Antibody and protein engineering
Most programs do not start from nothing. They start from a molecule that binds but is the wrong format, the wrong species, or carries a liability that will not survive development. This is the work of changing that molecule without losing what made it worth keeping.
What we change
- Format. Moving a binder between VHH, scFv, Fab, IgG and bispecific arrangements, including the linker and hinge choices that decide whether the new format behaves like the old one.
- Species. Humanization and germlining, with the framework moved toward germline only as far as the binding survives.
- Liabilities. Deamidation, isomerization, oxidation, free cysteines and glycosylation sequons removed from the framework, with the CDRs left alone unless a free thiol forces the issue.
- Affinity. In silico maturation proposing variants to test, rather than a claim that any of them is better before it is measured.
- Conjugation. Placing and testing cysteines for site-specific payload attachment, which is its own engineering problem and not a downstream detail.
Formats we work in
- VHH and nanobody
- scFv
- Fab
- Full-length IgG
- Bispecific and multivalent arrangements
- Non-antibody scaffolds and engineered proteins
How we check the change held
Every engineered molecule is folded and co-folded against its target, and screened for developability across the whole panel rather than a chosen few. Where the change is structural, molecular dynamics tells us whether the complex still holds. Nothing is called an improvement until it has been measured.