ArticleJournal of pharmaceutical sciences2018
Coformulation of Broadly Neutralizing Antibodies 3BNC117 and PGT121: Analytical Challenges During Preformulation Characterization and Storage Stability Studies.
Article in Journal of pharmaceutical sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Delivery devices and container closure systems for co-formulated and co-administered biologics.Antibody therapeutics · 2026Review
- Fate of Stressed Oligoclonal Antibodies Tracked by Fluorescence Cross-Correlation Spectroscopy: IgG Aggregation Proceeds across the Species Barrier.Analytical chemistry · 2025Article
- AI-based antibody discovery platform identifies novel, diverse, and pharmacologically active therapeutic antibodies against multiple SARS-CoV-2 strains.Antibody therapeutics · 2024Article
- Broadly neutralizing antibodies for HIV prevention: a comprehensive review and future perspectives.Clinical microbiology reviews · 2024Review
- Stable High-Concentration Monoclonal Antibody Formulations Enabled by an Amphiphilic Copolymer Excipient.Advanced therapeutics · 2023Article
- Stability Convergence in Antibody Coformulations.Molecular pharmaceutics · 2022Article
- Broadly Neutralizing Antibodies for HIV-1 Prevention.Frontiers in immunology · 2021Review
- Stability enhancement in a mAb and Fab coformulation.Scientific reports · 2020Article
- Advancements in the co-formulation of biologic therapeutics.Journal of controlled release : official journal of the Controlled Release Society · 2020Review
- Characterization of Co-Formulated High-Concentration Broadly Neutralizing Anti-HIV-1 Monoclonal Antibodies for Subcutaneous Administration.Antibodies (Basel, Switzerland) · 2020Article
- Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, we investigated analytical challenges associated with the formulation of 2 anti-HIV broadly neutralizing antibodies (bnAbs), 3BNC117 and PGT121, both separately at 100 mg/mL and together at 50 mg/mL each. The bnAb formulations were characterized for relative solubility and conformational stability followed by accelerated and real-time stability studies. Although the bnAbs were stable during 4°C storage, incubation at 40°C differentiated their stability profiles. Specific concentration-dependent aggregation rates at 30°C and 40°C were measured by size exclusion chromatography for the individual bnAbs with the mixture showing intermediate behavior. Interestingly, although the relative ratio of the 2 bnAbs remained constant at 4°C, the ratio of 3BNC117 to PGT121 increased in the dimer that formed during storage at 40°C. A mass spectrometry-based multiattribute method, identified and quantified differences in modifications of the Fab regions for each bnAb within the mixture including clipping, oxidation, deamidation, and isomerization sites. Each bnAb showed slight differences in the levels and sites of lysine residue glycations. Together, these data demonstrate the ability to differentiate degradation products from individual antibodies within the bnAb mixture, and that degradation rates are influenced not only by the individual bnAb concentrations but also by the mixture concentration.
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