Abstract
Since the time of the earliest jawed fish, some 400 million years ago, evolution has been honing the design of antibody molecules to function as specific markers, alerting immune defences to the presence of pathogenic antigens, and recruiting effector function in the form of complement and Fc receptor-bearing cells. For the last twenty-five years, the biopharmaceutical industry has been applying the versatility of antibodies to the treatment of disease, with roles ranging from the blocking of receptor/ligand interactions to the delivery of cytotoxic drugs. While the structures of antibody molecules are supremely tailored to carry out their natural roles, there is considerable scope for adapting the basic designs to match more closely the specific requirements now sought for antibodies as drugs. In this review, we chart the developments in antibody design, which have led to successful therapies, highlighting the key issues and challenges faced, and looking to a future in which antibody-based therapies will represent a significant proportion of newly registered products.
Keywords: antibody(ies), therapeutic, human(ized), recombinant, design, review
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