Affilin® molecules, like other scaffolds, combine the advantages of conventional antibodies with important features of small molecules. These features include high target affinity and specificity, small size, high stability, cost-effective manufacturing and amenability to genetic and chemical manipulations.
- As a natural human serum protein, the Affilin® scaffold Ubiquitin is nonimmunogenic. Additionally, it bears a built-in immunosuppressive peptide that further lowers the risk for immunogenic responses.
- The 100 % conservation of Ubiquitin scaffold in the animal world allows the straightforward development of final leads through all animal species without the need for surrogates. This supports rapid-development cycles comparable to small molecules.
- The natural Ubiquitin function in the proteasome pathway is used for the development of very effective Affilin® conjugates that display a new mechanism of action.
- The proprietary Multi Affilin® platform allows multimerization similar to naturally occurring Ubiquitin multimers yielding dimers (mono- and bispecific) as well as tetramers and octamers. This technology enables parallel multitargeting and adjustment of serum half-life.
- One Affilin® molecule enables multiple product developments by fusing or conjugating Affilin® molecules to effectors. Affilin® conjugates add new functionalities to blocking activity only.
- The extreme stability of the Ubiquitin scaffold and its complete lack of disulfide bonds and posttranslational modifications enable efficient microbial production and support Chemistry Manufacturing and Control (CMC) requirements.
- The Ubiquitin scaffold's stability in gastrointestinal fluid opens up the opportunity for oral routes of administration for the treatment of gastrointestinal disorders.
