FC VARIANTS HAVING IMPROVED PH-DEPENDENT FCRN BINDING CAPACITY AND FCGAMMA-RIIIA 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 capacity to selectively bind to Fcy receptors. 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 FcyRIIIa (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 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.