Abstract
Antibody-based drugs are increasingly used in the clinic, and their importance is set to escalate in the coming years as more drugs in this class progress through clinical trials. Although many such drugs utilize whole antibodies, others exploit fragments, e.g., fragment antigen binding (Fab′) or single-chain fragment variable (scFv), which retain the antigen-binding specificity without the fragment crystallizable (Fc) element necessary to mediate effector functions. Antibody fragments can be advantageous for many therapeutic uses, owing to the fact that valency and half-life can be tailored through protein engineering approaches to suit the desired mechanism of action (1). Furthermore, antibody fragments are more suited to expression in microbial systems, providing benefits in terms of increased scale and ease of manufacture (2).
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Popplewell, A.G., Sehdev, M., Spitali, M., Weir, A.N.C. (2005). Expression of Antibody Fragments by Periplasmic Secretion in Escherichia coli . In: Smales, C.M., James, D.C. (eds) Therapeutic Proteins. Methods in Molecular Biology™, vol 308. Humana Press. https://doi.org/10.1385/1-59259-922-2:017
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DOI: https://doi.org/10.1385/1-59259-922-2:017
Publisher Name: Humana Press
Print ISBN: 978-1-58829-390-9
Online ISBN: 978-1-59259-922-6
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