HUMAN FC VARIANTS HAVING IMPROVED FCGAMMA-RIIA BINDING SELECTIVITY

• Main Authors: KIM, Suyeon, KYUNG, Munsu, KO, Woo Hyung, JO, Migyeong, KO, Sanghwan, JUNG, Sang Taek
• Format: Patent
• Language: English; French; German
• Published: 28.08.2024
• Subjects: CHEMISTRY; HUMAN NECESSITIES; HYGIENE; MEDICAL OR VETERINARY SCIENCE; METALLURGY; ORGANIC CHEMISTRY; PEPTIDES; PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES; SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS ORMEDICINAL PREPARATIONS

The present invention relates to Fc variants which have improved half-life by binding to and unbinding from FcRn in a pH-dependent manner and which have improved selective binding to Fcyreceptors. Novel human Fc domain variants of the present invention have lower capacity to bind to immune inhibiting receptor FcyRIIb and have higher capacity to bind to immune activating receptor FcyRIIa (increased A/I ratio) than a wild-type human antibody Fc domain and conventional antibodies approved as antibody therapeutic agents, thereby having remarkably improved ADCP 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 so as 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 so as to be effectively used as an improved antibody drug.