ArticleBiophysical journal2007
Phase behavior of an intact monoclonal antibody.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- The Relationship between Protein-Protein Interactions and Liquid-Liquid Phase Separation for Monoclonal Antibodies.Molecular pharmaceutics · 2023Article
- On the Aggregation and Nucleation Mechanism of the Monoclonal Antibody Anti-CD20 Near Liquid-Liquid Phase Separation (LLPS).Scientific reports · 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
- Modeling the depletion effect caused by an addition of polymer to monoclonal antibody solutions.Journal of physics. Condensed matter : an Institute of Physics journal · 2018Article
- AUC measurements of diffusion coefficients of monoclonal antibodies in the presence of human serum proteins.European biophysics journal : EBJ · 2018Article
- Metastability Gap in the Phase Diagram of Monoclonal IgG Antibody.Biophysical journal · 2017Article
- Article
- Self-Interaction Chromatography of mAbs: Accurate Measurement of Dead Volumes.Pharmaceutical research · 2015Article
- Improving monoclonal antibody selection and engineering using measurements of colloidal protein interactions.Journal of pharmaceutical sciences · 2014Review
- Article
- Phase transitions in human IgG solutions.The Journal of chemical physics · 2013Article
- Non-aqueous suspensions of antibodies are much less viscous than equally concentrated aqueous solutions.Pharmaceutical research · 2013Article
- High-throughput analysis of concentration-dependent antibody self-association.Biophysical journal · 2011Article
- Article
- Liquid-liquid phase separation of a monoclonal antibody and nonmonotonic influence of Hofmeister anions.Biophysical journal · 2010Article
- Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation.Biophysical journal · 2010Article
- Phase separation of an IgG1 antibody solution under a low ionic strength condition.Pharmaceutical research · 2010Article
- Protein adsorption and transport in dextran-modified ion-exchange media. I: adsorption.Journal of chromatography. A · 2009Article
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- Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding protein phase behavior is important for purification, storage, and stable formulation of protein drugs in the biopharmaceutical industry. Glycoproteins, such as monoclonal antibodies (MAbs) are the most abundant biopharmaceuticals and probably the most difficult to crystallize among water-soluble proteins. This study explores the possibility of correlating osmotic second virial coefficient (B(22)) with the phase behavior of an intact MAb, which has so far proved impossible to crystallize. The phase diagram of the MAb is presented as a function of the concentration of different classes of precipitants, i.e., NaCl, (NH4)2SO4, and polyethylene glycol. All these precipitants show a similar behavior of decreasing solubility with increasing precipitant concentration. B(22) values were also measured as a function of the concentration of the different precipitants by self-interaction chromatography and correlated with the phase diagrams. Correlating phase diagrams with B(22) data provides useful information not only for a fundamental understanding of the phase behavior of MAbs, but also for understanding the reason why certain proteins are extremely difficult to crystallize. The scaling of the phase diagram in B(22) units also supports the existence of a universal phase diagram of a complex glycoprotein when it is recast in a protein interaction parameter.
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