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Annual Review of Biomedical Engineering

Volume 17, 2015

Advances in Antibody Design

Abstract

The use of monoclonal antibodies as therapeutics requires optimizing several of their key attributes. These include binding affinity and specificity, folding stability, solubility, pharmacokinetics, effector functions, and compatibility with the attachment of additional antibody domains (bispecific antibodies) and cytotoxic drugs (antibody–drug conjugates). Addressing these and other challenges requires the use of systematic design methods that complement powerful immunization and in vitro screening methods. We review advances in designing the binding loops, scaffolds, domain interfaces, constant regions, post-translational and chemical modifications, and bispecific architectures of antibodies and fragments thereof to improve their bioactivity. We also highlight unmet challenges in antibody design that must be overcome to generate potent antibody therapeutics.

Keyword(s): CDR, complementarity-determining region, Fab, IgG, scFv, VH
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/content/journals/10.1146/annurev-bioeng-071114-040733
2015-12-07
2024-04-26
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/content/journals/10.1146/annurev-bioeng-071114-040733
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Advances in Antibody Design
Annual Review of Biomedical Engineering 17, 191 (2015); https://doi.org/10.1146/annurev-bioeng-071114-040733
/content/journals/10.1146/annurev-bioeng-071114-040733
/content/journals/10.1146/annurev-bioeng-071114-040733
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