ArticleJournal of pharmaceutical sciences2008
High concentration formulations of recombinant human interleukin-1 receptor antagonist: I. Physical characterization.
Article in Journal of pharmaceutical sciences, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The trial behind it
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
9 citing papers in PubMed.
- On the Aggregation and Nucleation Mechanism of the Monoclonal Antibody Anti-CD20 Near Liquid-Liquid Phase Separation (LLPS).Scientific reports · 2020Article
- Protein-protein interactions controlling interfacial aggregation of rhIL-1ra are not described by simple colloid models.Protein science : a publication of the Protein Society · 2018Article
- Challenges in Predicting Protein-Protein Interactions from Measurements of Molecular Diffusivity.Biophysical journal · 2016Article
- Behavior of monoclonal antibodies: relation between the second virial coefficient (B (2)) at low concentrations and aggregation propensity and viscosity at high concentrations.Pharmaceutical research · 2012Article
- Effect of benzyl alcohol on recombinant human interleukin-1 receptor antagonist structure and hydrogen-deuterium exchange.Journal of pharmaceutical sciences · 2011Article
- Biodistribution, pharmacokinetics and metabolism of interleukin-1 receptor antagonist (IL-1RA) using [¹⁸F]-IL1RA and PET imaging in rats.British journal of pharmacology · 2011Article
- Static light scattering from concentrated protein solutions II: experimental test of theory for protein mixtures and weakly self-associating proteins.Biophysical journal · 2009Article
- Automated measurement of the static light scattering of macromolecular solutions over a broad range of concentrations.Analytical biochemistry · 2008Article
- Measurement of the second osmotic virial coefficient for protein solutions exhibiting monomer-dimer equilibrium.Analytical biochemistry · 2008Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
At relatively high protein concentrations (i.e., up to 100 mg/mL), recombinant human interleukin-1 receptor antagonist (rhIL-1ra) was found to exist in a monomer-dimer equilibrium controlled by solution ionic strength. Sedimentation equilibrium at 25 degrees C was used to measure the increase in the dimer dissociation constant (K(d)) as a function of ionic strength. K(d) increased from 2.0 to 12.6 mM as the solution ionic strength was increased from 0.011 to 0.184 molal. These K(d) values were used with both static light scattering and membrane osmometry data collected over a protein concentration range of 1-100 mg/mL to determine second osmotic virial coefficients. Expanding the second osmotic virial coefficient model to account for separate monomer-monomer (B(22)), monomer-dimer (B(23)), and dimer-dimer (B(33)) interactions reveals net monomer-dimer interactions are attractive, whereas the others are repulsive. Lastly, isothermal titration calorimetry dilution experiments showed that rhIL-1ra dimerization is enthalpically driven (DeltaH(dimerization) << 0), which is consistent with intermolecular cation-pi interactions previously proposed as the monomer-monomer contact sites in dimers.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.