Fc Engineering to Improve the Function of Therapeutic Antibodies

Author(s): Futa Mimoto, Taichi Kuramochi, Hitoshi Katada, Tomoyuki Igawa, Kunihiro Hattori

Journal Name: Current Pharmaceutical Biotechnology

Volume 17 , Issue 15 , 2016

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Monoclonal antibodies are currently the most attractive therapeutic modality in a broad range of disease areas, including infectious diseases, autoimmune diseases, and oncology. Fc engineering is one attractive application to maximize the value or overcome the drawbacks of monoclonal antibodies for therapeutic use. With the Fc region, antibodies bind to several types of receptors, such as Fc gamma receptors, a complement receptor, and a neonatal Fc receptor. Through this interaction with the receptors, antibodies demonstrate unique functions, such as antibody-dependent cellular cytotoxicity, antibody- dependent cellular phagocytosis, complement dependent cytotoxicity, agonistic activity, and endosomal recycling. Fc engineering technology is conducted mainly to maximize the receptor-mediated functions of antibodies. Moreover, Fc engineering of the two heavy chains to facilitate heterodimerization is indispensable for generating IgG-like bispecific antibodies that are asymmetric. Fc engineering is also conducted to avoid the undesired properties, such as cytokine release and protease-mediated cleavage of the hinge region, of wild-type antibodies, as well as providing additional functions. Thus, Fc engineering technology is an attractive approach for maximizing the potency and convenience of therapeutic antibodies. This review will cover a variety of Fc engineering technologies that improve the functions of therapeutic antibodies.

Keywords: Antibody engineering, therapeutic antibody, Fc engineering, antibody, protein engineering.

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Article Details

Year: 2016
Page: [1298 - 1314]
Pages: 17
DOI: 10.2174/1389201017666160824161854
Price: $65

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