ArticlePharmaceutical research2012
Behavior of monoclonal antibodies: relation between the second virial coefficient (B (2)) at low concentrations and aggregation propensity and viscosity at high concentrations.
Article in Pharmaceutical research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
50 citing papers in PubMed.
- Article
- Article
- Optical imaging and spectroscopic characterization of subvisible particles in protein therapeutics.Advanced drug delivery reviews · 2026Review
- Electrostatics and viscosity are strongly linked in concentrated antibody solutions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Impact of Weak Vibration Generated by a Refrigerator on Protein Aggregation.The AAPS journal · 2025Article
- A scaling relationship between thermodynamic and hydrodynamic interactions in protein solutions.Biophysical journal · 2024Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Exploring the Combined Action of Adding Pertuzumab to Branded Trastuzumab versus Trastuzumab Biosimilars for Treating HER2+ Breast Cancer.International journal of molecular sciences · 2024Article
- Article
- Role of Domain-Domain Interactions on the Self-Association and Physical Stability of Monoclonal Antibodies: Effect of pH and Salt.The journal of physical chemistry. B · 2023Article
- NMR Reveals Functionally Relevant Thermally Induced Structural Changes within the Native Ensemble of G-CSF.Molecular pharmaceutics · 2022Article
- Utility of High Resolution 2D NMR Fingerprinting in Assessing Viscosity of Therapeutic Monoclonal Antibodies.Pharmaceutical research · 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
- Probing interactions of therapeutic antibodies with serum via second virial coefficient measurements.Biophysical journal · 2021Article
- Application of Affinity-Capture Self-Interaction Nanoparticle Spectroscopy in Predicting Protein Stability, Especially for Co-Formulated Antibodies.Pharmaceutical research · 2021Article
- Global multi-method analysis of interaction parameters for reversibly self-associating macromolecules at high concentrations.Scientific reports · 2021Article
- Characterization and Modeling of Reversible Antibody Self-Association Provide Insights into Behavior, Prediction, and Correction.Antibodies (Basel, Switzerland) · 2021Article
- Washing with alkaline solutions in protein A purification improves physicochemical properties of monoclonal antibodies.Scientific reports · 2021Article
- A single molecular descriptor to predict solution behavior of therapeutic antibodies.Science advances · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeTo investigate relationship between second virial coefficient B (2) and viscosity and aggregation propensity of highly concentrated monoclonal antibody (MAbs) solutions.
methodsIntermolecular interactions of 3 MAbs solutions with varying pH were characterized according to B (2) estimated by analytical ultracentrifugation sedimentation equilibrium with initial loading concentrations <10 mg/mL. Viscosity measurements and stability assessments of MAb solutions at concentrations higher than 100 mg/mL were conducted.
resultsB (2) of all MAb solutions depended on solution pH and have qualitative correlation with viscosity and aggregation propensity. The more negative the B (2) values, the more viscous the solution, acquiring increased propensity to aggregate. Solutions with B (2) values of ~2 × 10(-5) mL·mol/g(2) acquire similar viscosity and aggregation propensity regardless of amino acid sequences; for solutions with negative B (2) values, viscosity and aggregation propensity differed depending on sequences. Results suggest attractive intermolecular interactions represented by negative B (2) values are influenced by surface properties of individual MAbs.
conclusionsB (2) can be used, within certain limitations, as an effective indicator of viscosity and aggregation propensity of highly concentrated MAb solutions.
Indexed as
Identifiers
21853361What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.