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Their small size helps access difficult-to-reach therapeutic targets on tissues and cells as well as penetrate tumours more effectively.1,2 These small fragments can also be useful for rapidly blocking signalling molecules or receptors. Because they do not have the bulk of a whole antibody, fragments can also minimise other downstream effects on the immune system.1
Fragment antibodies are emerging as great tools in imaging and diagnostics because they are capable of detecting cellular proteins with high affinity and specificity. They can be easily linked to radioisotopes, fluorescent molecules or enzymes that tag specific biomarkers in patients. They also have a shorter half-life in the body which results in faster clearance and may result in fewer risks of side effects from potentially invasive diagnostic agents.
Fragment antibodies can also be produced in simpler steps compared with more complex antibodies, making them potentially faster to produce in high yields.
1. Bates, Adam, and Christine A. Power. 2019. “David vs. Goliath: The Structure, Function, and Clinical Prospects of Antibody Fragments.” Antibodies (Basel, Switzerland) 8 (2). http://doi.org/10.3390/antib8020028.
2. Kholodenko, Roman V., Daniel V. Kalinovsky, Igor I. Doronin, Eugene D. Ponomarev, and Irina V. Kholodenko. 2019. “Antibody Fragments as Potential Biopharmaceuticals for Cancer Therapy: Success and Limitations.” Current Medicinal Chemistry 26 (3): 396–426.
If you believe in the power of what science can do, join us in our endeavour to push the boundaries of science to deliver life-changing medicines.
We know that however innovative our science, however effective our medicines and delivery, to achieve all we want to achieve, we cannot do it alone.
Veeva ID: Z4-46776
Date of preparation: August 2022