ArticleBiotechnology progress
A comparative study of monoclonal antibodies. 1. Phase behavior and protein-protein interactions.
Article in Biotechnology progress. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The trial behind it
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Who cites it
11 citing papers in PubMed.
- Temperature and excipient mediated modulation of monoclonal antibody interactions revealed bymAbs · 2025Article
- Prediction of Self-Association and Solution Behavior of Monoclonal Antibodies Using the QCM-D Metric of Loosely Interacting Layer.Molecular pharmaceutics · 2025Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- EPR Viscometric Measurements Using aApplied magnetic resonance · 2023Article
- The Relationship between Protein-Protein Interactions and Liquid-Liquid Phase Separation for Monoclonal Antibodies.Molecular pharmaceutics · 2023Article
- Nanocrystalline protein domains via salting-out.Acta crystallographica. Section F, Structural biology communications · 2021Article
- A single molecular descriptor to predict solution behavior of therapeutic antibodies.Science advances · 2020Article
- Theory for the Liquid-Liquid Phase Separation in Aqueous Antibody Solutions.The journal of physical chemistry. B · 2018Article
- Determinants of protein elution rates from preparative ion-exchange adsorbents.Journal of chromatography. A · 2016Article
- A comparative study of monoclonal antibodies. 1. Phase behavior and protein-protein interactions.Biotechnology progressArticle
- Downstream Processing Technologies/Capturing and Final Purification : Opportunities for Innovation, Change, and Improvement. A Review of Downstream Processing Developments in Protein Purification.Advances in biochemical engineering/biotechnologyReview
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Protein phase behavior is involved in numerous aspects of downstream processing, either by design as in crystallization or precipitation processes, or as an undesired effect, such as aggregation. This work explores the phase behavior of eight monoclonal antibodies (mAbs) that exhibit liquid-liquid separation, aggregation, gelation, and crystallization. The phase behavior has been studied systematically as a function of a number of factors, including solution composition and pH, in order to explore the degree of variability among different antibodies. Comparisons of the locations of phase boundaries show consistent trends as a function of solution composition; however, changing the solution pH has different effects on each of the antibodies studied. Furthermore, the types of dense phases formed varied among the antibodies. Protein-protein interactions, as reflected by values of the osmotic second virial coefficient, are used to correlate the phase behavior. The primary findings are that values of the osmotic second virial coefficient are useful for correlating phase boundary locations, though there is appreciable variability among the antibodies in the apparent strengths of the intrinsic protein-protein attraction manifested. However, the osmotic second virial coefficient does not provide a clear basis to predict the type of dense phase likely to result under a given set of solution conditions.
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Registered trials
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