ArticlePharmaceutical research2010
Phase separation of an IgG1 antibody solution under a low ionic strength condition.
Article in Pharmaceutical research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Electrostatic bimodality of human cytosolic DNA sensor cGAS-dsDNA condensates revealed by millisecond flashing electrophoretic separation.Nature communications · 2026Article
- Molecular origins of opalescence and phase separation in mAb formulations and their relation to aggregation.Communications chemistry · 2026Article
- BiFC and FACS-based CRISPR screening revealed that QKI promotes PABPN1 LLPS in colorectal cancer cells.Protein & cell · 2025Article
- Growth of Clusters toward Liquid-Liquid Phase Separation of Monoclonal Antibodies as Characterized by Small-Angle X-ray Scattering and Molecular Dynamics Simulation.The journal of physical chemistry. B · 2025Article
- Comprehensive Regulation of Liquid-Liquid Phase Separation of Polypeptides.Molecules (Basel, Switzerland) · 2023Article
- Mass photometric detection and quantification of nanoscale α-synuclein phase separation.Nature chemistry · 2023Article
- Comparative Thermodynamics of the Reversible Self-Association of Therapeutic mAbs Reveal Opposing Roles for Linked Proton- and Ion-Binding Events.Pharmaceutical research · 2023Article
- The Relationship between Protein-Protein Interactions and Liquid-Liquid Phase Separation for Monoclonal Antibodies.Molecular pharmaceutics · 2023Article
- Recombinant antibodies aggregation and overcoming strategies in CHO cells.Applied microbiology and biotechnology · 2022Review
- Comprehensive Assessment of Protein and Excipient Stability in Biopharmaceutical Formulations UsingACS pharmacology & translational science · 2021Article
- Energetic Dissection of Mab-Specific Reversible Self-Association Reveals Unique Thermodynamic Signatures.Pharmaceutical research · 2021Article
- Estimating and leveraging protein diffusion on ion-exchange resin surfaces.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mitigation of liquid-liquid phase separation of a monoclonal antibody by mutations of negative charges on the Fab surface.PloS one · 2020Article
- Employing Flow Cytometry to Extracellular Vesicles Sample Microvolume Analysis and Quality Control.Frontiers in cell and developmental biology · 2020Article
- Methods for Physical Characterization of Phase-Separated Bodies and Membrane-less Organelles.Journal of molecular biology · 2018Review
- Theory for the Liquid-Liquid Phase Separation in Aqueous Antibody Solutions.The journal of physical chemistry. B · 2018Article
- Sedimentation velocity analytical ultracentrifugation for characterization of therapeutic antibodies.Biophysical reviews · 2018Review
- A new approach to quantification of mAb aggregates using peptide affinity probes.Scientific reports · 2017Article
- Antibody Aggregation: Insights from Sequence and Structure.Antibodies (Basel, Switzerland) · 2016Review
- Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposePhase separation of monoclonal antibody A (MAb A) solution and its relation to protein self-association are studied.
methodsA phase diagram of MAb A and its dependence on ionic strength and pH were investigated. The protein self-associations were characterized by dynamic light scattering (DLS), analytical ultracentrifugation analysis (AUC) and viscosity measurement.
resultsMAb A solution with a clear appearance in an isotonic ionic strength condition turned opalescent in a low ionic strength condition, followed by liquid-liquid phase separation (LLPS) into light and heavy phases. The protein concentrations of the two phases were dependent on the ionic strength and pH. The two phases became reversibly miscible when the ionic strength or temperature was increased. DLS and AUC showed that MAb A under a low ionic strength condition self-associates at a protein concentration above the critical concentration of 16.5 mg/mL. The viscosity of the heavy phase was high and dependent on the shear rate. These results indicate that attractive protein-protein interaction in the heavy phase induces LLPS.
conclusionsLLPS was induced in MAb A solution in a low ionic strength condition due to reversible protein self-association mediated mainly by attractive electrostatic interaction among the MAb A molecules in the heavy phase.
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