ArticlemAbs2016
Extending the half-life of a fab fragment through generation of a humanized anti-human serum albumin Fv domain: An investigation into the correlation between affinity and serum half-life.
Article in mAbs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 67 citations in OpenAlex.
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- Biophysical analysis of angiotensin II and amyloid-β cross-interaction in aggregation and membrane disruption.FEBS letters · 2026Article
- SurfDiff: protein surface profiling for selective or broadly reactive epitope prioritisation in binder and immunogen design.bioRxiv : the preprint server for biology · 2025Article
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- Protein-Based Degraders: From Chemical Biology Tools to Neo-Therapeutics.Chemical reviews · 2025Review
- Effectors of the Future: Universal Chimeric Antigen Receptor.Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie · 2025Review
- Improved safety of chimeric antigen receptor T cells indirectly targeting antigens via switchable adapters.Nature communications · 2024Article
- Impact of tissue penetration and albumin binding on design of T cell targeted bispecific agents.Neoplasia (New York, N.Y.) · 2024Article
- Crystal structure of human serum albumin in complex with megabody reveals unique human and murine cross-reactive binding site.Protein science : a publication of the Protein Society · 2024Article
- Serum immunoglobulin or albumin binding single-domain antibodies that enable tailored half-life extension of biologics in multiple animal species.Frontiers in immunology · 2024Article
- Development of [EJNMMI research · 2023Article
- Albumin binding improves nanobody pharmacokinetics for dual-modality PET/NIRF imaging of CEACAM5 in colorectal cancer models.European journal of nuclear medicine and molecular imaging · 2023Article
- Serum albumin binding knob domains engineered within a VFrontiers in immunology · 2023Article
- Smaller size packs a stronger punch - Recent advances in small antibody fragments targeting tumour-associated carbohydrate antigens.Theranostics · 2023Review
- Modification of the structural stability of human serum albumin in rheumatoid arthritis.PloS one · 2023Article
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We generated an anti-albumin antibody, CA645, to link its Fv domain to an antigen-binding fragment (Fab), thereby extending the serum half-life of the Fab. CA645 was demonstrated to bind human, cynomolgus, and mouse serum albumin with similar affinity (1-7 nM), and to bind human serum albumin (HSA) when it is in complex with common known ligands. Importantly for half-life extension, CA645 binds HSA with similar affinity within the physiologically relevant range of pH 5.0 - pH 7.4, and does not have a deleterious effect on the binding of HSA to neonatal Fc receptor (FcRn). A crystal structure of humanized CA645 Fab in complex with HSA was solved and showed that CA645 Fab binds to domain II of HSA. Superimposition with the crystal structure of FcRn bound to HSA confirmed that CA645 does not block HSA binding to FcRn. In mice, the serum half-life of humanized CA645 Fab is 84.2 h. This is a significant extension in comparison with < 1 h for a non-HSA binding CA645 Fab variant. The Fab-HSA structure was used to design a series of mutants with reduced affinity to investigate the correlation between the affinity for albumin and serum half-life. Reduction in the affinity for MSA by 144-fold from 2.2 nM to 316 nM had no effect on serum half-life. Strikingly, despite a reduction in affinity to 62 µM, an extension in serum half-life of 26.4 h was still obtained. CA645 Fab and the CA645 Fab-HSA complex have been deposited in the Protein Data Bank (PDB) with accession codes, 5FUZ and 5FUO, respectively.
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