ArticleJournal of molecular liquids2022
The influence of excipients on the viscosity of monoclonal antibody solutions.
Article in Journal of molecular liquids, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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.
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Who cites it
7 citing papers in PubMed.
- Engineering the subcutaneous delivery of antibody-drug conjugates.Journal of controlled release : official journal of the Controlled Release Society · 2026Article
- Designing for medication adherence in inflammatory bowel disease: multi-disciplinary approaches for self-administrable biotherapeutics.EClinicalMedicine · 2024Review
- One-Step Air Spraying of Structural Coating on Cu Alloy as Superhydrophobic Surface for Enhanced Corrosion Resistance and Anti-Icing Performance.Materials (Basel, Switzerland) · 2024Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Alkalinity Regulation and Optimization of Cementitious Materials Used in Ecological Porous Concrete.Materials (Basel, Switzerland) · 2024Article
- Study on the Preparation and Properties of Vegetation Lightweight Porous Concrete.Materials (Basel, Switzerland) · 2024Article
- Protein Association in Solution: Statistical Mechanical Modeling.Biomolecules · 2023Review
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
The aggregation propensity of monoclonal antibodies can be modified by adding different cosolutes into the solution. A simple coarse-grained model in the combination with the thermodynamic perturbation theory was used to predict cluster distribution and viscosity of the solutions of IgG4 monoclonal anibody in the presence of L-Arginine Hydrochloride. The data were analysed using binding polynomial to describe the binding of cosolute (Arginine) to the antibody molecule. The results show that by binding to the antibody molecule the cosolute occupies some of the binding sites of the antibody, and in this way reduces the amount of binding sites available to other antibody molecules. The aggregation propensity of the antibody molecules is therefore reduced.
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Registered trials
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