ArticleBiophysical journal2002
Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 215 citations in OpenAlex.
- Quantitative Perspectives of Biomolecular Crystallization Thermodynamics.Advances in biochemical engineering/biotechnology · 2026Review
- Stabilising proteins in solution using affordable and readily available small molecules.Biophysical reviews · 2025Review
- Modulating Weak Protein-Protein Cross-Interactions by the Addition of Free Amino Acids at Millimolar Concentrations.The journal of physical chemistry. B · 2024Article
- Protein translational diffusion as a way to detect intermolecular interactions.Biophysical reviews · 2023Review
- Effects of Monovalent Salt on Protein-Protein Interactions of Dilute and Concentrated Monoclonal Antibody Formulations.Antibodies (Basel, Switzerland) · 2022Article
- Measuring Self-Association of Antibody Lead Candidates with Dynamic Light Scattering.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Assessment of Therapeutic Antibody Developability by Combinations of In Vitro and In Silico Methods.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Conformational Ensembles of Antibodies Determine Their Hydrophobicity.Biophysical journal · 2021Article
- A Reappraisal of Sedimentation Nonideality Coefficients for the Analysis of Weak Interactions of Therapeutic Proteins.The AAPS journal · 2019Article
- Improved adsorption reactions, kinetics and stability for model and therapeutic proteins immobilised on affinity resins.Adsorption : journal of the International Adsorption Society · 2019Article
- Chromatographic parameter determination for complex biological feedstocks.Biotechnology progress · 2018Article
- Effect of the surface charge distribution on the fluid phase behavior of charged colloids and proteins.The Journal of chemical physics · 2016Article
- Explicit-water theory for the salt-specific effects and Hofmeister series in protein solutions.The Journal of chemical physics · 2016Article
- A Discontinuous Potential Model for Protein-Protein Interactions.Foundations of Molecular Modeling and Simulation : select papers from FOMMS 2015. International Conference on Foundations of Molecular Modeling and Simulation (6th : 2015 : Mount Hood, Or.) · 2016Article
- Self-Interaction Chromatography of mAbs: Accurate Measurement of Dead Volumes.Pharmaceutical research · 2015Article
- The second virial coefficient as a predictor of protein aggregation propensity: A self-interaction chromatography study.European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V · 2015Article
- Determination of the second virial coefficient of bovine serum albumin under varying pH and ionic strength by composition-gradient multi-angle static light scattering.Journal of biological physics · 2015Article
- Article
- Membrane proteins, detergents and crystals: what is the state of the art?Acta crystallographica. Section F, Structural biology communications · 2014Review
- Protein solubilization: a novel approach.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Weak protein interactions are often characterized in terms of the osmotic second virial coefficient (B(22)), which has been shown to correlate with protein phase behavior, such as crystallization. Traditional methods for measuring B(22), such as static light scattering, are too expensive in terms of both time and protein to allow extensive exploration of the effects of solution conditions on B(22). In this work we have measured protein interactions using self-interaction chromatography, in which protein is immobilized on chromatographic particles and the retention of the same protein is measured in isocratic elution. The relative retention of the protein reflects the average protein interactions, which we have related to the second virial coefficient via statistical mechanics. We obtain quantitative agreement between virial coefficients measured by self-interaction chromatography and traditional characterization methods for both lysozyme and chymotrypsinogen over a wide range of pH and ionic strengths, yet self-interaction chromatography requires at least an order of magnitude less time and protein than other methods. The method thus holds significant promise for the characterization of protein interactions requiring only commonly available laboratory equipment, little specialized expertise, and relatively small investments of both time and protein.
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