ArticlemAbs
Measuring aggregates, self-association, and weak interactions in concentrated therapeutic antibody solutions.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Hydrodynamic and thermodynamic analysis of PEGylated human serum albumin.Biophysical journal · 2024Article
- The origins of nonideality exhibited by monoclonal antibodies and Fab fragments in human serum.Protein science : a publication of the Protein Society · 2023Article
- An automated interface for sedimentation velocity analysis in SEDFIT.PLoS computational biology · 2023Article
- Lymphocyte activation gene 3 is increased and affects cytokine production in rheumatoid arthritis.Arthritis research & therapy · 2023Article
- An automated interface for sedimentation velocity analysis in SEDFIT.bioRxiv : the preprint server for biology · 2023Article
- The Relationship between Protein-Protein Interactions and Liquid-Liquid Phase Separation for Monoclonal Antibodies.Molecular pharmaceutics · 2023Article
- Best Practices for Aggregate Quantitation of Antibody Therapeutics by Sedimentation Velocity Analytical Ultracentrifugation.Journal of pharmaceutical sciences · 2022Review
- Effects of Monovalent Salt on Protein-Protein Interactions of Dilute and Concentrated Monoclonal Antibody Formulations.Antibodies (Basel, Switzerland) · 2022Article
- Nanoencapsulation as a General Solution for Lyophilization of Labile Substrates.Pharmaceutics · 2021Article
- Characterization of DNA-protein complexes by nanoparticle tracking analysis and their association with systemic lupus erythematosus.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Global multi-method analysis of interaction parameters for reversibly self-associating macromolecules at high concentrations.Scientific reports · 2021Article
- A case study showing the role of hydrophobicity variants and other enriched mAb proteoforms on filterability through a virus filter with productivity improvement measures.Biotechnology progressArticle
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Monoclonal antibodies are a class of biotherapeutics used for an increasing variety of disorders, including cancer, autoimmune, neurodegenerative, and viral diseases. Besides their antigen specificity, therapeutic use also mandates control of their solution interactions and colloidal properties in order to achieve a stable, efficacious, non-immunogenic, and low viscosity antibody solution at concentrations in the range of 50-150 mg/mL. This requires characterization of their reversible self-association, aggregation, and weak attractive and repulsive interactions governing macromolecular distance distributions in solution. Simultaneous measurement of these properties, however, has been hampered by solution nonideality. Based on a recently introduced sedimentation velocity method for measuring macromolecular size distributions in a mean-field approximation for hydrodynamic interactions, we demonstrate simultaneous measurement of polydispersity and weak and strong solution interactions in a panel of antibodies with concentrations up to 45 mg/mL. By allowing approximately an order of magnitude higher concentrations than previously possible in sedimentation velocity size distribution analysis, this approach can substantially improve efficiency and sensitivity for characterizing polydispersity and interactions of therapeutic antibodies at or close to formulation conditions.
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