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Extending Serum Half-life of Albumin by Engineering Neonatal Fc Receptor (FcRn) Binding
Open accessAbstract
A major challenge for the therapeutic use of many peptides and proteins is their short circulatory half-life. Albumin has an extended serum half-life of 3 weeks because of its size and FcRn-mediated recycling that prevents intracellular degradation, properties shared with IgG antibodies. Engineering the strictly pH-dependent IgG-FcRn interaction is known to extend IgG half-life. However, this principle has not been extensively explored for albumin. We have engineered human albumin by introducing single point mutations in the C-terminal end that generated a panel of variants with greatly improved affinities for FcRn. One variant (K573P) with 12-fold improved affinity showed extended serum half-life in normal mice, mice transgenic for human FcRn, and cynomolgus monkeys. Importantly, favorable binding to FcRn was maintained when a single-chain fragment variable antibody was genetically fused to either the N- or the C-terminal end. The engineered albumin variants may be attractive for improving the serum half-life of biopharmaceuticals.
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Metadata
- Authors
- Andersen, J. T., Dalhus, B., Viuff, D., Ravn, B. T., Gunnarsen, K. S., Plumridge, A., Bunting, K., Antunes, F., Williamson, R., Athwal, S., Allan, E., Evans, L., Bjørås, M., Kjærulff, S., Sleep, D., Sandlie, I., & Cameron, J.
- Affiliations
- University of Oslo (NO)
- Oslo University Hospital (NO)
- Novozymes (United Kingdom) (GB)
- Novozymes (Denmark) (DK)
- Corresponding author
- Andersen, Jan Terje
- Cameron, Jason
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2014-05
- Volume
- 289
- Issue
- 19
- Pages
- 13492-13502
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC4036356
- OpenAlex
- W2088696708
- Cited by
- 167
- References
- 37
- Citations by year
- 2026: 12 · 2025: 13 · 2024: 11 · 2023: 14 · 2022: 12 · 2021: 22 · 2020: 15 · 2019: 11 · 2018: 16 · 2017: 9 · 2016: 14 · 2015: 13 · 2014: 5
- FWCI
- 10.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- NORA - Norwegian Open Research Archives (submittedVersion, other-oa)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- human serum albumin, neonatal Fc receptor, serum half-life, albumin variants, scFv, Macaca fascicularis, biopharmaceuticals
- MeSH terms
- Albumins, Animals, Female, Half-Life, Humans, Macaca fascicularis, Receptors, Fc, Recombinant Fusion Proteins, Histocompatibility Antigens Class I, Amino Acid Substitution, Mutation, Missense, Mice
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