期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1844, 期 11, 页码 1977-1982出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2014.04.018
关键词
Monoclonal antibody; Domain antibody; Antibody engineering; Monomeric Fc; CH3 domain; CH2 domain
资金
- Intramural Research Program of the NIH, National Cancer Institute, Center for Cancer Research
- Federal funds from the NIH, National Cancer Institute [NO1-CO-12400, HHSN261200800001E]
- CRADA
- RCT
- Wuhan Key Laboratory on Emerging Infectious Diseases and Biosafety
Therapeutic monoclonal antibodies (mAbs) have been successful for the therapy of a number of diseases mostly cancer and immune disorders. However, the vast majority of mAbs approved for clinical use are full size, typically in IgG1 format. These mAbs may exhibit relatively poor tissue penetration and restricted epitope access due to their large size. A promising solution to this fundamental limitation is the engineering of smaller scaffolds based on the IgG1 Fc region. These scaffolds can be used for the generation of libraries of mutants from which high-affinity binders can be selected. Comprised of the CH2 and CH3 domains, the Fc region is important not only for the antibody effector function but also for its long half-life. This review focuses on engineered Fc based antibody fragments and domains including native (dimeric) Fc and monomeric Fc as well as CH2 and monomeric CH3, and their use as novel scaffolds and binders. The Fc based binders are promising candidate therapeutics with optimized half-life, enhanced tissue penetration and access to sterically restricted binding sites resulting in an increased therapeutic efficacy. This article is part of a Special Issue entitled: Recent advances in molecular engineering of antibody. Published by Elsevier B.V.
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