ArticleMolecular pharmaceutics2019
Studying Excipient Modulated Physical Stability and Viscosity of Monoclonal Antibody Formulations Using Small-Angle Scattering.
Article in Molecular pharmaceutics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 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
23 citing papers in PubMed, 60 citations in OpenAlex.
- Article
- Article
- Article
- Review
- 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
- Understanding the Impacts of Molecular and Macromolecular Crowding Agents on Protein-Polymer Complex Coacervates.Biomacromolecules · 2023Article
- 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
- Effects of arginine in therapeutic protein formulations: a decade review and perspectives.Antibody therapeutics · 2023Review
- Stability of Monoclonal Antibodies as Solid Formulation for Auto-Injectors: A Pilot Study.Pharmaceutics · 2023Article
- Enabling Efficient Design of Biological Formulations Through Advanced Characterization.Pharmaceutical research · 2023Review
- Analytical Workflows to Unlock Predictive Power in Biotherapeutic Developability.Pharmaceutical research · 2023Article
- Amino acid-mPEGs: Promising excipients to stabilize human growth hormone against aggregation.Iranian journal of basic medical sciences · 2023Article
- Accelerating therapeutic protein design with computational approaches toward the clinical stage.Computational and structural biotechnology journal · 2023Review
- Effects of Monovalent Salt on Protein-Protein Interactions of Dilute and Concentrated Monoclonal Antibody Formulations.Antibodies (Basel, Switzerland) · 2022Article
- A General Small-Angle X-ray Scattering-Based Screening Protocol for Studying Physical Stability of Protein Formulations.Pharmaceutics · 2021Article
- Revisit PEG-Induced Precipitation Assay for Protein Solubility Assessment of Monoclonal Antibody Formulations.Pharmaceutical research · 2021Article
- Global multi-method analysis of interaction parameters for reversibly self-associating macromolecules at high concentrations.Scientific reports · 2021Article
- Cetuximab-conjugated perfluorohexane/gold nanoparticles for low intensity focused ultrasound diagnosis ablation of thyroid cancer treatment.Science and technology of advanced materials · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Excipients are substances that are added to therapeutic products to improve stability, bioavailability, and manufacturability. Undesirable protein-protein interactions (PPI) can lead to self-association and/or high solution viscosity in concentrated protein formulations that are typically greater than 50 mg/mL. Therefore, understanding the effects of excipients on nonspecific PPI is important for more efficient formulation development. In this study, we used National Institute of Standards and Technology monoclonal antibody (NISTmAb) reference material as a model antibody protein to examine the physical stability and viscosity of concentrated formulations using a series of excipients, by varying pH, salt composition, and the presence of cosolutes including amino acids, sugars, and nonionic surfactants. Small angle X-ray scattering (SAXS) together with differential scanning calorimetry (DSC), dynamic light scattering (DLS), and viscosity measurements were used to obtain various experimental parameters to characterize excipient modulated PPI and bulk solution viscosities. In particular, a good correlation was found between SAXS and DLS/SLS results, suggesting that the use of DLS/SLS is valid for predicting the colloidal stability of NISTmAb in concentrated solutions. Moreover, further analysis of effective structure factor
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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.