Antibody Engineering


Over the years, we investigated and engineered stable antibody frameworks with significantly better properties than natural ones. This work lead to such a stability-engineered antibody against EpCAM being now in clinical trials.

Also, extremely tight binders were evolved in vitro against proteins, peptides and small molecules, up to 1 pM (a monovalent scFv against the prion protein). It is usually impossible to obtain such high affinities from immunized animals, but it is now possible from libraries, using directed evolution.

Very fundamental questions can be asked in this fascinating protein family: How does nature design diversity? What features need to be preserved to maintain the integrity of the fold? Do these features play an equivalent role when the proteins are made in different formats and in prokaryotic or eukaryotic cells? What features are engineered into the molecule that prevent aggregation? Clearly, the answers to these questions not only are of fundamental interest, but also have immediate applications in the creation of molecules that are even better suited for the many uses of antibodies.