ArticlemAbs
A comparison of biophysical characterization techniques in predicting monoclonal antibody stability.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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.
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
45 citing papers in PubMed, 116 citations in OpenAlex.
- Article
- Article
- A Review on the Stability Challenges of Advanced Biologic Therapeutics.Pharmaceutics · 2025Review
- Rationalizing mAb Candidate Screening Using a Single Holistic Developability Parameter.Molecular pharmaceutics · 2025Article
- Mapping conformational changes on bispecific antigen-binding biotherapeutic by covalent labeling and mass spectrometry.Journal of pharmaceutical analysis · 2024Article
- Extrapolating differential scanning calorimetry data for monoclonal antibodies to low temperatures.Analytical biochemistry · 2024Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Taurine, a Naturally Occurring Amino Acid, as a Physical Stability Enhancer of Different Monoclonal Antibodies.The AAPS journal · 2024Article
- Production of Antibodies to Peptide Targets Using Hybridoma Technology.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Site-Specific Structural Changes in Long-Term-Stressed Monoclonal Antibody Revealed with DEPC Covalent-Labeling and Quantitative Mass Spectrometry.Pharmaceuticals (Basel, Switzerland) · 2023Article
- COVID-19 impedimetric biosensor based on polypyrrole nanotubes, nickel hydroxide and VHH antibody fragment: specific, sensitive, and rapid viral detection in saliva samples.Materials today. Chemistry · 2023Article
- Lot-to-Lot Variance in Immunoassays-Causes, Consequences, and Solutions.Diagnostics (Basel, Switzerland) · 2023Review
- Bioprocess Development and Characterization of aAntibodies (Basel, Switzerland) · 2023Article
- A Review of Protein- and Peptide-Based Chemical Conjugates: Past, Present, and Future.Pharmaceutics · 2023Review
- Advancing humanized monoclonal antibody for counteracting fentanyl toxicity towards clinical development.Human vaccines & immunotherapeutics · 2022Article
- Challenges and Strategies for a Thorough Characterization of Antibody Acidic Charge Variants.Bioengineering (Basel, Switzerland) · 2022Article
- NMR Reveals Functionally Relevant Thermally Induced Structural Changes within the Native Ensemble of G-CSF.Molecular pharmaceutics · 2022Article
- Hydroxylpropyl-β-cyclodextrin as Potential Excipient to Prevent Stress-Induced Aggregation in Liquid Protein Formulations.Molecules (Basel, Switzerland) · 2022Article
- Stability of the Retinoid X Receptor-α Homodimer in the Presence and Absence of Rexinoid and Coactivator Peptide.Biochemistry · 2021Article
- Application of Affinity-Capture Self-Interaction Nanoparticle Spectroscopy in Predicting Protein Stability, Especially for Co-Formulated Antibodies.Pharmaceutical research · 2021Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
With the rapid growth of biopharmaceutical product development, knowledge of therapeutic protein stability has become increasingly important. We evaluated assays that measure solution-mediated interactions and key molecular characteristics of 9 formulated monoclonal antibody (mAb) therapeutics, to predict their stability behavior. Colloidal interactions, self-association propensity and conformational stability were measured using effective surface charge via zeta potential, diffusion interaction parameter (kD) and differential scanning calorimetry (DSC), respectively. The molecular features of all 9 mAbs were compared to their stability at accelerated (25°C and 40°C) and long-term storage conditions (2-8°C) as measured by size exclusion chromatography. At accelerated storage conditions, the majority of the mAbs in this study degraded via fragmentation rather than aggregation. Our results show that colloidal stability, self-association propensity and conformational characteristics (exposed tryptophan) provide reasonable prediction of accelerated stability, with limited predictive value at 2-8°C stability. While no correlations to stability behavior were observed with onset-of-melting temperatures or domain unfolding temperatures, by DSC, melting of the Fab domain with the CH2 domain suggests lower stability at stressed conditions. The relevance of identifying appropriate biophysical assays based on the primary degradation pathways is discussed.
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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.