ArticleProceedings of the National Academy of Sciences of the United States of America2011
Phase separation in solutions of monoclonal antibodies and the effect of human serum albumin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
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
25 citing papers in PubMed, 80 citations in OpenAlex.
- Testing mixing rules for structural and dynamical quantities in multi-component crowded protein solutions.APL bioengineering · 2024Article
- Protein Association in Solution: Statistical Mechanical Modeling.Biomolecules · 2023Review
- The Relationship between Protein-Protein Interactions and Liquid-Liquid Phase Separation for Monoclonal Antibodies.Molecular pharmaceutics · 2023Article
- Conformational Changes and Drivers of Monoclonal Antibody Liquid-Liquid Phase Separation.Journal of pharmaceutical sciences · 2023Article
- Revisit PEG-Induced Precipitation Assay for Protein Solubility Assessment of Monoclonal Antibody Formulations.Pharmaceutical research · 2021Article
- The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021Review
- Multivalent ions and biomolecules: Attempting a comprehensive perspective.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020Review
- Spatially Resolved Effects of Protein Freeze-Thawing in a Small-Scale Model Using Monoclonal Antibodies.Pharmaceutics · 2020Article
- Mitigation of liquid-liquid phase separation of a monoclonal antibody by mutations of negative charges on the Fab surface.PloS one · 2020Article
- Framework Mutations of the 10-1074 bnAb Increase Conformational Stability, Manufacturability, and Stability While Preserving Full Neutralization Activity.Journal of pharmaceutical sciences · 2020Article
- A stepwise mechanism for aqueous two-phase system formation in concentrated antibody solutions.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- ICA512 RESP18 homology domain is a protein-condensing factor and insulin fibrillation inhibitor.The Journal of biological chemistry · 2019Article
- Evaluating the Effects of Hinge Flexibility on the Solution Structure of Antibodies at Concentrated Conditions.Journal of pharmaceutical sciences · 2019Article
- Article
- Why Do Disordered and Structured Proteins Behave Differently in Phase Separation?Trends in biochemical sciences · 2018Review
- Theory for the Liquid-Liquid Phase Separation in Aqueous Antibody Solutions.The journal of physical chemistry. B · 2018Article
- Liquid-Liquid Phase Separation of Patchy Particles Illuminates Diverse Effects of Regulatory Components on Protein Droplet Formation.Scientific reports · 2018Article
- Metastability Gap in the Phase Diagram of Monoclonal IgG Antibody.Biophysical journal · 2017Article
- Modeling phase transitions in mixtures of β-γ lens crystallins.Soft matter · 2016Article
- Fast Method for Computing Chemical Potentials and Liquid-Liquid Phase Equilibria of Macromolecular Solutions.The journal of physical chemistry. B · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report the observation of liquid-liquid phase separation in a solution of human monoclonal antibody, IgG2, and the effects of human serum albumin, a major blood protein, on this phase separation. We find a significant reduction of phase separation temperature in the presence of albumin, and a preferential partitioning of the albumin into the antibody-rich phase. We provide a general thermodynamic analysis of the antibody-albumin mixture phase diagram and relate its features to the magnitude of the effective interprotein interactions. Our analysis suggests that additives (HSA in this report), which have moderate attraction with antibody molecules, may be used to forestall undesirable protein condensation in antibody solutions. Our findings are relevant to understanding the stability of pharmaceutical solutions of antibodies and the mechanisms of cryoglobulinemia.
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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.