Betamab uses its proprietary platform technology, betabodies, for discovery and development of highly specific extracellular and intracellular protein-protein inhibitors.
In contrast to all other technologies such as e.g. monoclonal antibodies, peptides, or other binder technologies, betabodies are designed in-silico and not by selection from chemical or biological libraries. The only requirement for designing betabodies is knowledge about the target 3D structure. Because of the use of combinatorial in-silico screening, the 2-3 kDA small betabodies can, therefore, be synthesized from unnatural L and D amino acids. This raises the betabody theoretical and exploitable binding diversity to incredibly 1037. Consequently, betabodies are protease-resistant and possess very low immunogenicity. Betamab introduces rational drug design into protein-protein-inhibitors.
The betabody in-silico design is possible because of their unusual highly predictable structural stability due to the presence of hydrophilic threonine side chains on one side of the beta-hairpin.
Three betabodies against IL-1β
Betamab has successfully designed betabodies against a dozen different extracellular and intracellular proteins. We design two types of betabodies which optionally also contain cell-penetrating properties. One class of betabodies is designed for interaction with protein surfaces and the other class interacts with protein grooves and pits.