ArticlePharmaceutical research2013
Effects of ionic strength and sugars on the aggregation propensity of monoclonal antibodies: influence of colloidal and conformational stabilities.
Article in Pharmaceutical research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 103 citations in OpenAlex.
- Preventing physical and chemical degradation of the LABL-Fc-MOGAntibody therapeutics · 2026Article
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Quantitative Analysis and Predictive Modeling of Nonspecific Adsorption of Recombinant Adeno-Associated Virus onto Solid Surfaces.Langmuir : the ACS journal of surfaces and colloids · 2026Article
- A Review on the Stability Challenges of Advanced Biologic Therapeutics.Pharmaceutics · 2025Review
- Antibody Aggregation: A Problem Within the Biopharmaceutical Industry and Its Role in AL Amyloidosis Disease.The protein journal · 2025Review
- A case study of a bispecific antibody manufacturability assessment and optimization during discovery stage and its implications.Antibody therapeutics · 2024Article
- Enhanced Thermal Stability and Reduced Aggregation in an Antibody Fab Fragment at Elevated Concentrations.Molecular pharmaceutics · 2023Article
- Alternative Excipients for Protein Stabilization in Protein Therapeutics: Overcoming the Limitations of Polysorbates.Pharmaceutics · 2022Review
- Aggregation Time Machine: A Platform for the Prediction and Optimization of Long-Term Antibody Stability Using Short-Term Kinetic Analysis.Journal of medicinal chemistry · 2022Article
- Impact of enzymatic reduction on bivalent bispecific antibody fragmentation and loss of product purity upon reoxidation.Biotechnology and bioengineering · 2020Article
- Mitigation of liquid-liquid phase separation of a monoclonal antibody by mutations of negative charges on the Fab surface.PloS one · 2020Article
- Characterizing and Minimizing Aggregation and Particle Formation of Three Recombinant Fusion-Protein Bulk Antigens for Use in a Candidate Trivalent Rotavirus Vaccine.Journal of pharmaceutical sciences · 2020Article
- Article
- Bilateral Effects of Excipients on Protein Stability: Preferential Interaction Type of Excipient and Surface Aromatic Hydrophobicity of Protein.Pharmaceutical research · 2017Article
- Article
- Recent applications of light scattering measurement in the biological and biopharmaceutical sciences.Analytical biochemistry · 2016Review
- Assessment of the Protein-Protein Interactions in a Highly Concentrated Antibody Solution by Using Raman Spectroscopy.Pharmaceutical research · 2016Article
- Direct analysis of mAb aggregates in mammalian cell culture supernatant.BMC biotechnology · 2014Article
- The effect of arginine glutamate on the stability of monoclonal antibodies in solution.International journal of pharmaceutics · 2014Article
- High-throughput biophysical analysis of protein therapeutics to examine interrelationships between aggregate formation and conformational stability.The AAPS journal · 2014Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeTo develop a general strategy for optimizing monoclonal antibody (MAb) formulations.
methodsColloidal stabilities of four representative MAbs solutions were assessed based on the second virial coefficient (B 2) at 20°C and 40°C, and net charges at different NaCl concentrations, and/or in the presence of sugars. Conformational stabilities were evaluated from the unfolding temperatures. The aggregation propensities were determined at 40°C and after freeze-thawing. The electrostatic potential of antibody surfaces was simulated for the development of rational formulations.
resultsSimilar B 2 values were obtained at 20°C and 40°C, implying little dependence on temperature. B 2 correlated quantitatively with aggregation propensities at 40°C. The net charge partly correlated with colloidal stability. Salts stabilized or destabilized MAbs, depending on repulsive or attractive interactions. Sugars improved the aggregation propensity under freeze-thaw stress through improved conformational stability. Uneven and even distributions of potential surfaces were attributed to attractive and strong repulsive electrostatic interactions.
conclusionsAssessment of colloidal stability at the lowest ionic strength is particularly effective for the development of formulations. If necessary, salts are added to enhance the colloidal stability. Sugars further improved aggregation propensities by enhancing conformational stability. These behaviors are rationally predictable according to the surface potentials of MAbs.
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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.