Abstract
In the past three decades, bispecific antibodies have taken center stage as one of the most fiercely expanding classes of the antibody-based therapeutic reagents. Apart of performing two tasks in one, their inherently linked two specificities were found to be able to initiate novel biological effects, unpreceded in biological phenomena such as engaging effector cells to act against tumor cells, replacing a missing link in an enzyme cascade, or acting as molecular Trojan horses to exert their activity in otherwise inaccessible cellular compartments, tissues, and organs. These unique modes of action have triggered the interest of the protein engineering community to harvest the versatility and plasticity of immunoglobulin-based molecules and to design a plethora of fusion-based, homodimeric and heterodimeric architectures, as well as to refine the parameters of their heterologous expression, downstream processing, and analytics. With these developments, the design of the molecular species optimally functional for a particular biological situation appears to be at reach even for multispecific and multivalent formats, limited only by researcher’s imagination.
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Wozniak-Knopp, G. (2021). Bispecific Antibodies. In: Rüker, F., Wozniak-Knopp, G. (eds) Introduction to Antibody Engineering. Learning Materials in Biosciences. Springer, Cham. https://doi.org/10.1007/978-3-030-54630-4_7
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