ArticlePharmaceutical research2017
Contrasting the Influence of Cationic Amino Acids on the Viscosity and Stability of a Highly Concentrated Monoclonal Antibody.
Article in Pharmaceutical research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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.
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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
23 citing papers in PubMed, 68 citations in OpenAlex.
- Delivery devices and container closure systems for co-formulated and co-administered biologics.Antibody therapeutics · 2026Review
- Temperature and excipient mediated modulation of monoclonal antibody interactions revealed bymAbs · 2025Article
- Monoclonal antibody formulations: a quantitative analysis of marketed products and patents.mAbs · 2025Article
- Electrostatics and viscosity are strongly linked in concentrated antibody solutions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Developing high-concentration monoclonal antibody formulations for subcutaneous administration to improve patient treatment.Biophysical reviews · 2025Review
- A Review on the Stability Challenges of Advanced Biologic Therapeutics.Pharmaceutics · 2025Review
- Growth of Clusters toward Liquid-Liquid Phase Separation of Monoclonal Antibodies as Characterized by Small-Angle X-ray Scattering and Molecular Dynamics Simulation.The journal of physical chemistry. B · 2025Article
- Rapid Development of High Concentration Protein Formulation Driven by High-Throughput Technologies.Pharmaceutical research · 2025Article
- Leveraging high-throughput analytics and automation to rapidly develop high-concentration mAb formulations: integrated excipient compatibility and viscosity screening.Antibody therapeutics · 2024Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Poly(glutamic acid)-Based Viscosity Reducers for Concentrated Formulations of a Monoclonal IgG Antibody.Molecular pharmaceutics · 2024Article
- Protein Association in Solution: Statistical Mechanical Modeling.Biomolecules · 2023Review
- Microfluidic techniques for mechanical measurements of biological samples.Biophysics reviews · 2023Review
- The influence of excipients on the viscosity of monoclonal antibody solutions.Journal of molecular liquids · 2022Article
- Discovery of compounds with viscosity-reducing effects on biopharmaceutical formulations with monoclonal antibodies.Computational and structural biotechnology journal · 2022Article
- A microfluidic approach to studying the injection flow of concentrated albumin solutions.SN applied sciences · 2021Article
- Assessment of Antibody Self-Interaction by Bio-Layer-Interferometry as a Tool for Early Stage Formulation Development.Pharmaceutical research · 2020Article
- Controlling the viscosities of antibody solutions through control of their binding sites.Journal of molecular liquids · 2018Article
- Theory for the Liquid-Liquid Phase Separation in Aqueous Antibody Solutions.The journal of physical chemistry. B · 2018Article
- Improving Viscosity and Stability of a Highly Concentrated Monoclonal Antibody Solution with Concentrated Proline.Pharmaceutical research · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeTo explain the effects of cationic amino acids and other co-solutes on the viscosity, stability and protein-protein interactions (PPI) of highly concentrated (≥200 mg/ml) monoclonal antibody (mAb) solutions to advance subcutaneous injection.
methodsThe viscosities of ≥200 mg/ml mAb1 solutions with various co-solutes and pH were measured by capillary rheometry in some cases up to 70,000 s
resultsViscosity reductions were achieved by reducing the pH, or adding histidine, arginine, imidazole or camphorsulfonic acid, each of which contains a hydrophobic moiety. The addition of inorganic electrolytes or neutral osmolytes only weakly affected viscosity. Systems with reduced viscosities also tended to be Newtonian, while more viscous systems were shear thinning.
conclusionsViscosity reduction down to 20 cP at 220 mg/ml mAb1 was achieved with co-solutes that are both charged and contain a hydrophobic interaction domain for sufficient binding to the protein surface. These reductions are related to the DLS diffusion interaction parameter, k
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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.