期刊
ANNUAL REVIEW OF BIOMEDICAL ENGINEERING, VOL 17
卷 17, 期 -, 页码 191-216出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-bioeng-071114-040733
关键词
IgG; scFv; V-H; Fab; CDR; complementarity-determining region
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM104130] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM104130, R01GM104130] Funding Source: Medline
- Directorate For Engineering [1159943, 0954450] Funding Source: National Science Foundation
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. Wereview 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.
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