ArticleJournal of pharmaceutical sciences2005
Aggregation kinetics of recombinant human FVIII (rFVIII).
Article in Journal of pharmaceutical sciences, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 21 citations in OpenAlex.
- Native-like aggregates of factor VIII are immunogenic in von Willebrand factor deficient and hemophilia a mice.Journal of pharmaceutical sciences · 2012Article
- Phosphatidylinositol containing lipidic particles reduces immunogenicity and catabolism of factor VIII in hemophilia a mice.The AAPS journal · 2010Article
- Use of a folding model and in situ spectroscopic techniques for rational formulation development and stability testing of monoclonal antibody therapeutics.Journal of pharmaceutical sciences · 2010Article
- Role of glycosylation in conformational stability, activity, macromolecular interaction and immunogenicity of recombinant human factor VIII.The AAPS journal · 2009Article
- O-phospho-L-serine, multi-functional excipient for B domain deleted recombinant factor VIII.The AAPS journal · 2007Article
- Interaction of dicaproyl phosphatidylserine with recombinant factor VIII and its impact on immunogenicity.The AAPS journal · 2006Article
- Influence of aggregation on immunogenicity of recombinant human Factor VIII in hemophilia A mice.Journal of pharmaceutical sciences · 2006Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The physical phenomenon of aggregation can have profound impact on the stability of therapeutic proteins. This study focuses on the aggregation behavior of recombinant human FVIII (rFVIII), a multi-domain protein used as the first line of therapy for hemophilia A, a bleeding disorder caused by the deficiency or dysfunction of factor VIII (FVIII). Thermal denaturation of rFVIII was investigated using circular dichroism (CD) spectroscopy and size exclusion chromatography (SEC). The dependence of unfolding on heating rate indicated that the thermal denaturation of the protein was at least partly under kinetic control. The data was interpreted in terms of a simple two-state kinetic model, N(Native) k --> A(Aggregated), where k is a first-order kinetic constant that changes with temperature, as given by the Arrhenius equation. Analysis of the data in terms of the above scheme suggested that under the experimental conditions used in this study, the rate-controlling step in the aggregation of rFVIII may be a unimolecular reaction involving conformational changes.
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Registered trials
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