Boosting therapeutic potency of antibodies by taming Fc domain functions
강태현, 정상택,
소속 상세정보
강태현 ( Kang Tae-Hyun )
Kookmin University School of Applied Chemistry Biopharmaceutical Chemistry Major
정상택 ( Jung Sang-Taek )
Korea University Graduate School of Medicine Department of Biomedical Sciences
Abstract
Monoclonal antibodies (mAbs) are one of the most widely used drug platforms for infectious diseases or cancer therapeutics because they selectively target pathogens, infectious cells, cancerous cells, and even immune cells. In this way, they mediate the elimination of target molecules and cells with fewer side effects than other therapeutic modalities. In particular, cancer therapeutic mAbs can recognize cell-surface proteins on target cells and then kill the targeted cells by multiple mechanisms that are dependent upon a fragment crystallizable (Fc) domain interacting with effector Fc gamma receptors, including antibody-dependent cell-mediated cytotoxicity and antibody-dependent cell-mediated phagocytosis. Extensive engineering efforts have been made toward tuning Fc functions by either reinforcing (e.g. for targeted therapy) or disabling (e.g. for immune checkpoint blockade therapy) effector functions and prolonging the serum half-lives of antibodies, as necessary. In this report, we review Fc engineering efforts to improve therapeutic potency, and propose future antibody engineering directions that can fulfill unmet medical needs.
키워드
Antibody therapy; Drug development
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SCI(E)
MEDLINE
KCI
KoreaMed
KAMS