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Designing Two-In-One Antibodies
Immunotherapy, 2009Evaluation of: Bostrom J, Shang-Fan Y, Kan D et al.: Variants of the antibody Herceptin that interact with HER2 and VEGF at the antigen binding site. Science 323, 1610-1614 (2009). The longstanding held notion that one antibody equals one antigen and, hence, one function has been challenged in recent years.
Ignacio Garcia, Valladares +1 more
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Structure-Guided Design of Antibodies
Current Computer Aided-Drug Design, 2010Monoclonal antibodies capable of recognizing antigens with high affinity and specificity represent a wellestablished class of biological agents. Since the development of hybridoma technology in 1975, advances in recombinant DNA technologies and computational and biophysical methods have allowed us to develop a better understanding of the relationships ...
Justin A, Caravella +3 more
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Clinical issues in antibody design
Trends in Biotechnology, 1995Antibody genes can now be cloned and expressed in various ways to give new versions of antibodies that possess reduced immunogenicity, improved affinity, altered size, increased avidity and novel effector functions. The task for any clinical application is, first, to define a relevant target, and then to design the optimal antibody-based therapeutic ...
K A, Chester, R E, Hawkins
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Antibody Modeling: Implications for Engineering and Design
Methods, 2000Our understanding of the rules relating sequence to structure in antibodies has led to the development of accurate knowledge-based procedures for antibody modeling. Information gained from the analysis of antibody structures has been successfully exploited to engineer antibody-like molecules endowed with prescribed properties, such as increased ...
Morea V, Lesk, AM, Tramontano, A
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Potent antibody therapeutics by design
Nature Reviews Immunology, 2006Antibodies constitute the most rapidly growing class of human therapeutics and the second largest class of drugs after vaccines. The generation of potent antibody therapeutics, which I review here, is an iterative design process that involves the generation and optimization of antibodies to improve their clinical potential.
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Design of synthetic antibody libraries
Expert Opinion on Biological Therapy, 2007Antibody libraries came into existence 15 years ago when the accumulating sequence data of immunoglobulin genes and the advent of polymerase chain reaction technology made it possible to clone antibody gene repertoires. Since then, virtually hundreds of antibody libraries have been constructed, employing limitless maneuvers from the antibody ...
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A Novel Monoclonal Antibody Design for Radioimmunotherapy
Cancer Biotherapy and Radiopharmaceuticals, 2003The generation of chimeric and complementary-determining region (CDR) grafted monoclonal antibodies (MAb) have reduced the immunogenicity problem in the clinical application of radioimmunotherapy with monoclonal antibodies. However, humanization (Hu) has prolonged the circulation (plasma T1/2) of radiolabeled antibodies, resulting in an increased ...
Andres, Forero +7 more
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Toward aggregation-resistant antibodies by design
Trends in Biotechnology, 2013Monoclonal antibodies are attractive therapeutics for treating a wide range of human disorders due to their exquisite binding specificity and high binding affinity. However, a limitation of antibodies is their highly variable and difficult-to-predict propensities to aggregate when concentrated during purification and delivery.
Christine C, Lee +2 more
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Rational Design of Antibody Protease Inhibitors
Journal of the American Chemical Society, 2015The bovine antibody BLV1H12, which has an ultralong CDR3H, provides a novel scaffold for engineering new functions into the antibody's variable region. By modifying the β-strand "stalk" of BLV1H12 with sequences derived from natural or synthetic protease inhibitors, we have generated antibodies that inhibit bovine trypsin and human neutrophil elastase (
Tao, Liu +7 more
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Designing stable humanized antibodies
Nature Biomedical Engineering, 2023Alissa M. Hummer, Charlotte M. Deane
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