The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
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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“This occurs at a lower rate in health.22”
From Hypoalbuminemia: Pathogenesis and Clinical Significance (2019) · cites this paper as [22]
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Cites
Crystal structure of human serum albumin at 2.5 Å resolution
Sugio, S., Kashima, A., Mochizuki, S., Noda, M., & Kobayashi, K. (1999) · Protein Engineering Design and Selection · doi:10.1093/protein/12.6.439 · Cited by 1,816
Curry, S., Mandelkow, H., Brick, P., & Franks, N. P. (1998) · Nature Structural Biology · doi:10.1038/1869 · Cited by 1,378
Quantitative analysis of protein far UV circular dichroism spectra by neural networks
Böhm, G., Muhr, R., & Jaenicke, R. (1992) · Protein Engineering Design and Selection · doi:10.1093/protein/5.3.191 · Cited by 1,114
Impact of albumin on drug delivery — New applications on the horizon
Elsadek, B., & Kratz, F. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2011.09.069 · Cited by 853
Therapeutic antibodies for autoimmunity and inflammation
Chan, A. C., & Carter, P. J. (2010) · Nature reviews. Immunology · doi:10.1038/nri2761 · Cited by 846
Enhanced antibody half-life improves in vivo activity
Zalevsky, J., Chamberlain, A. K., Horton, H. M., Karki, S., Leung, I., Sproule, T. J., Lazar, G. A., Roopenian, D. C., & Desjarlais, J. R. (2010) · Nature Biotechnology · doi:10.1038/nbt.1601 · Cited by 667
Chaudhury, C., Mehnaz, S., Robinson, J. M., Hayton, W. L., Pearl, D. K., Roopenian, D. C., & Anderson, C. L. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021829 · Cited by 640
Albumin as a versatile platform for drug half-life extension
Sleep, D., Cameron, J., & Evans, L. R. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.023 · Cited by 510
Self-citationCrystal structural analysis of human serum albumin complexed with hemin and fatty acid
Zunszain, P. A., Ghuman, J., Komatsu, T., Tsuchida, E., & Curry, S. (2003) · BMC Structural Biology · doi:10.1186/1472-6807-3-6 · Cited by 509
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Cited by
Sorted by citations
Hypoalbuminemia: Pathogenesis and Clinical Significance
Soeters, P. B., Wolfe, R. R., & Shenkin, A. (2019) · Journal of Parenteral and Enteral Nutrition · doi:10.1002/jpen.1451 · Cited by 1,448
Albumin-based drug delivery: harnessing nature to cure disease
Larsen, M. T., Kuhlmann, M., Hvam, M. L., & Howard, K. A. (2016) · Molecular and Cellular Therapies · doi:10.1186/s40591-016-0048-8 · Cited by 704
Fusion Proteins for Half-Life Extension of Biologics as a Strategy to Make Biobetters
Strohl, W. R. (2015) · BioDrugs · doi:10.1007/s40259-015-0133-6 · Cited by 479
Albumin and its application in drug delivery
Sleep, D. (2014) · Expert Opinion on Drug Delivery · doi:10.1517/17425247.2015.993313 · Cited by 470
Self-citationThe Neonatal Fc Receptor (FcRn): A Misnomer?
Pyzik, M., Sand, K. M. K., Hubbard, J. J., Andersen, J. T., Sandlie, I., & Blumberg, R. S. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01540 · Cited by 450
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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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