The science behind VHH antibodies.
VHHs are a lot like antibodies but smaller, simpler, and more robust. Originally isolated from camelid species in the 1990s, these proteins represent the antigen binding region (VH domain) of a Heavy chain-only antibody.
Some VHHs were trademarked as “nanobodies” by the company Ablynx in 2003, who also launched the first FDA-approved VHH drug, caplacizumab.
As a result, VHHs are often also referred to as nanobodies. These early drugs were discovered using llama immunisations, but at Isogenica we mine our Synthetic VHH Libraries for pre-humanised leads using well-characterised, pre-defined frameworks.
At around 10% of the size of a traditional monoclonal antibody, VHHs display the same highly sensitive and specific binding. Because all this binding is concentrated into a single protein unit, they are very simple proteins – easy to make rapidly from microbial or mammalian systems.
Unlike full-length antibodies, they do not naturally form pairs and prefer to exist in a monomeric, soluble form – ideal for therapeutics manufacture.
They are also not associated with complex immune modulatory functions which some full IgG therapies suffer from.
The big reason that Isogenica sees VHHs as special is their flexibility. Because of their simplicity, they can easily link to other biomolecules, including other VHHs, for numerous applications.
With a decade of synthetic VHH discovery campaigns under our belt, Isogenica is building on this expertise to develop internal drug assets for oncology. To explore the many different therapeutic and diagnostic uses for VHHs, including Isogenica’s multi-specifics pipeline, check out our Applications pages.
Isogenica ISOXTEND® half-life extension for biotherapeutics
Our VHH-based ISOXTEND® technology protects biotherapeutics from kidney clearance by ‘piggybacking’ onto the serum albumin endocytic recycling pathway, significantly extending therapeutic half-life.