Dual action to improve target specificity


Bispecific antibodies (BiSAbs) are unique in their ability to bind to two different targets at the same time. The two different epitopes (the part of the target that the antibody attaches to) to which the BiSAb binds can either be found on the same target, or the BiSAb can bind to two separate targets, each containing a distinct epitope. This dual action principle makes BiSAbs an interesting approach to improve target specificity.1

We want to unlock the full potential of BiSAbs as targeted therapeutics. Through precise target selection, we are exploring the use of BiSAbs to engage the immune system to destroy tumour cells, to deliver cytotoxic drugs to tumours, or to block vital signalling pathways in oncology and other disease areas.2 One area of emerging significance is the potential value of these targeted agents in treatment of refractory or resistant forms of cancer, a growing challenge in oncology.3

We are also at the forefront of developing innovative platforms for constructing BiSAbs that fulfil stringent purity and stability criteria. These platforms give us greater flexibility to design many possible combinations of antibodies, proteins and small molecules with desired characteristics. This assembly kit approach to drug design grants our scientists promising prospects for novel biopharmaceuticals.


We are innovating beyond current immunotherapies by engineering candidate drugs that coordinate multiple complimentary immune mechanisms with an aim to improving patients’ ability to fight cancer.

Daniel Freeman Vice President, Early Oncology, Immunotherapy, Cell Therapy and Antibody Drug Conjugates

References

1. Suurs, Frans V., Marjolijn N. Lub-de Hooge, Elisabeth G. E. de Vries, and Derk Jan A. de Groot. 2019. “A Review of Bispecific Antibodies and Antibody Constructs in Oncology and Clinical Challenges.” Pharmacology & Therapeutics 201 (September): 103–19.

2. Ali SO, Yu XQ, Robbie GJ, et al. Phase 1 study of MEDI3902, an investigational anti-Pseudomonas aeruginosa PcrV and Psl bispecific human monoclonal antibody, in healthy adults. Clin Microbiol Infect. 2019;25(5):629.e1-629.e6. doi:10.1016/j.cmi.2018.08.004.

3. Tran, B et al. P308 33rd Annual Meeting & Pre-Conference Programs of the Society for Immunotherapy of Cancer (SITC 2018). Available at: https://jitc.bmj.com/content/7/1/46.



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