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    FC ALPHA RECEPTOR BINDING ANTIBODY
    1.
    发明公开
    FC ALPHA RECEPTOR BINDING ANTIBODY 审中-公开

    公开(公告)号：US20230399407A1

    公开(公告)日：2023-12-14

    申请号：US18035609

    申请日：2021-11-03

    Applicant: KOREA UNIVERSITY RESEARCH AND BUSINESS FOUNDATION

    Inventor： Sang Taek JUNG ,  Ji Sun LEE ,  Bo Mi KIM

    IPC: C07K16/28 ,  C07K16/32

    CPC classification number: C07K16/283 ,  C07K16/32 ,  C07K2317/92 ,  C07K2317/31 ,  C07K2317/622

    Abstract: The present invention relates to an antibody having enhanced binding affinity for human Fc alpha receptor and a technique for maximizing a mechanism of antibody action by using same. Antibodies specific for Fc alpha receptors or immunologically active fragments thereof according to the present invention are in the form of IgG and bind to Fc alpha receptors of effector cells, especially, neutrophils, which are most abundant in mammals, thereby overcoming the disadvantages of conventional IgA antibodies and maximizing an effector function in various antibody therapeutic agents, which leads to maximizing the mechanism of antibody action (ADCC and ADCP). Thus, various Fc-fused protein therapeutic agents using same can be advantageously utilized as antibody drugs with enhanced effector functions.

    FC VARIANTS HAVING IMPROVED PH-DEPENDENT FCRN BINDING CAPACITY AND FCRIIIA BINDING SELECTIVITY
    2.
    发明申请
    FC VARIANTS HAVING IMPROVED PH-DEPENDENT FCRN BINDING CAPACITY AND FCRIIIA BINDING SELECTIVITY 有权

    公开(公告)号：US20240425612A1

    公开(公告)日：2024-12-26

    申请号：US18702227

    申请日：2022-10-17

    Applicant: KOREA UNIVERSITY RESEARCH AND BUSINESS FOUNDATION

    Inventor： Sang Taek JUNG ,  Munsu KYUNG ,  Sanghwan KO ,  Migyeong JO ,  Suyeon KIM ,  Woo Hyung KO

    IPC: C07K16/32 ,  A61K47/68

    Abstract: Provided are Fc variants having improved half-life by binding to and unbinding from FcRn in a pH-dependent manner, which have improved capacity to selectively bind to Fcγ receptors. The human Fc domain variants have lower capacity to bind to immune-inhibiting receptor FcγRIIb and have higher capacity to bind to immune activating receptor FcγRIIIa (increased A/I ratio) than a wild-type human antibody Fc domain and conventional antibodies approved as antibody therapeutic agents, thereby having remarkably improved ADCC induction ability and having maximized half-life in blood in which excellent pH-selective FcRn binding and unbinding capacity is exhibited, and thus bind to numerous peptide drug therapeutics having a low half-life and retention time in the body to enable the peptide drug therapeutics to have an increased blood half-life and exhibit long-term drug efficacy, and can maximize the immune mechanism of therapeutic protein drugs to be effectively used as an improved antibody drug.

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