Engineering FcRn binding kinetics dramatically extends antibody serum half-life and enhances therapeutic potential
This study presents a rational Fc engineering framework to optimize FcRn binding kinetics, addressing a previously unconsidered challenge-endogenous IgG competition during intracellular trafficking of therapeutic antibodies. The distinct kinetic behaviors of YML and EML highlight the critical necessity of precise control over pH-dependent association and dissociation rates in FcRn binding. YML represents a next-generation Fc platform, offering enhanced pharmacokinetics and improved effector functions, thus providing a powerful strategy for developing biologics with superior serum persistence and therapeutic efficacy.
Authors
- Byoung Joon Ko (ORCID: https://orcid.org/0000-0001-9841-4022)
- Wonju Lee (ORCID: https://orcid.org/0000-0002-6836-0745)
- Young‐Jin Chun (ORCID: https://orcid.org/0000-0002-1438-8152)
- Munsu Kyung
- Sang Taek Jung (ORCID: https://orcid.org/0000-0001-7217-979X)
- Jung‐Hyun Na (ORCID: https://orcid.org/0000-0002-5257-2428)
- Sanghwan Ko (ORCID: https://orcid.org/0000-0002-2950-4937)
- Migyeong Jo (ORCID: https://orcid.org/0000-0001-8035-7461)
- Woo Hyung Ko
Institutions
- Seoul National University (KR)
- Korea University (KR)
- National University (SD)
- Korea University (JP)
Publication Details
- Journal
- Journal of Biological Engineering
- Published
- 2025-04-18
- DOI
- https://doi.org/10.1186/s13036-025-00506-y
- Citations
- 7
- Primary Topic
- Monoclonal and Polyclonal Antibodies Research
- Type
- article
- Field-Weighted Citation Impact
- 9.52
Funders
- National Research Foundation
- Ministry of Health and Welfare
- National Research Foundation of Korea
- Korea Drug Development Fund
- Ministry of Science and ICT, South Korea