ArticleThe AAPS journal2007
O-phospho-L-serine, multi-functional excipient for B domain deleted recombinant factor VIII.
Article in The AAPS journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Immune tolerance platforms to mitigate unwanted immune responses.Journal of pharmaceutical sciences · 2026Review
- Immune regulatory adjuvant approach to mitigate subcutaneous immunogenicity of monoclonal antibodies.Frontiers in immunology · 2024Article
- Stable binding to phosphatidylserine-containing membranes requires conserved arginine residues in tandem C domains of blood coagulation factor VIII.Frontiers in molecular biosciences · 2022Article
- Immunogenicity Challenges Associated with Subcutaneous Delivery of Therapeutic Proteins.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2021Review
- Immunogenicity of Protein Pharmaceuticals.Journal of pharmaceutical sciences · 2019Review
- Effects of hypertonic buffer composition on lymph node uptake and bioavailability of rituximab, after subcutaneous administration.Biopharmaceutics & drug disposition · 2015Article
- Intravenous administration of Factor VIII-O-Phospho-L-Serine (OPLS) complex reduces immunogenicity and preserves pharmacokinetics of the therapeutic protein.European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences · 2015Article
- Native-like aggregates of factor VIII are immunogenic in von Willebrand factor deficient and hemophilia a mice.Journal of pharmaceutical sciences · 2012Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Factor VIII (FVIII) is an important cofactor in the blood coagulation cascade. A deficiency or dysfunction of FVIII causes hemophilia A, a life-threatening bleeding disorder. FVIII circulates in plasma as a heterodimer comprising 6 domains (heavy chain, A1-A2-B and light chain, A3-C1-C2). Replacement therapy using FVIII is the leading therapy in the management of hemophilia A. However, approximately 15% to 30% of patients develop inhibitory antibodies that neutralize the activity of the protein. Neutralizing antibodies to epitopes in the lipid binding region of FVIII are commonly identified in patients' plasma. In this report, we investigated the effect of O-phospho-L-serine (OPLS), which binds to the lipid binding region, on the immunogenicity of B domain deleted recombinant factor VIII (BDDrFVIII). Sandwich enzyme-linked immunosorbent assay (ELISA) studies showed that OPLS specifically bind to the lipid binding region, localized in the C2 domain of the coagulation factor. Size exclusion chromatography and fluorescence anisotropy studies showed that OPLS interfered with the aggregation of BDDrFVIII. Immunogenicity of free- vs BDDrFVIII-OPLS complex was evaluated in a murine model of hemophilia A. Animals administered subcutaneous (sc) injections of BDDrFVIII-OPLS had lower neutralizing titers compared with animals treated with BDDrFVIII alone. Based on these studies, we hypothesize that specific molecular interactions between OPLS and BDDrFVIII may improve the stability and reduce the immunogenicity of BDDrFVIII formulations.
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Registered trials
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