ArticlemAbs
Molecular computations of preferential interactions of proline, arginine.HCl, and NaCl with IgG1 antibodies and their impact on aggregation and viscosity.
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Who cites it
21 citing papers in PubMed, 44 citations in OpenAlex.
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- Cosolute effects reveal the nature of weak forces governing GLP-1 oligomer stability.The Journal of biological chemistry · 2026Article
- Fab-Fc and Fab-Fab interactions of variable strength and valency contribute to the high concentration viscosity of IgGProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Monoclonal antibody formulations: a quantitative analysis of marketed products and patents.mAbs · 2025Article
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- Review
- Development of production methodologies for scFv-Fc conjugated critical reagents to support CAR-T clinical programs.Bioanalysis · 2025Article
- A Convenient Strategy for Studying Antibody Aggregation and Inhibition of Aggregation: Characterization and Simulation.Pharmaceutics · 2025Article
- Machine learning driven acceleration of biopharmaceutical formulation development using Excipient Prediction Software (ExPreSo).Computational and structural biotechnology journal · 2025Article
- In situ crystalline structure of the human eosinophil major basic protein-1.bioRxiv : the preprint server for biology · 2024Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Understanding the Specific Implications of Amino Acids in the Antibody Development.The protein journal · 2024Review
- Effects of arginine in therapeutic protein formulations: a decade review and perspectives.Antibody therapeutics · 2023Review
- Tuning charge density of chimeric antigen receptor optimizes tonic signaling and CAR-T cell fitness.Cell research · 2023Article
- Ionic Liquid-Based Strategy for Predicting Protein Aggregation Propensity and Thermodynamic Stability.JACS Au · 2022Article
- An experimental approach probing the conformational transitions and energy landscape of antibodies: a glimmer of hope for reviving lost therapeutic candidates using ionic liquid.Chemical science · 2021Article
- Article
- Variable domain mutational analysis to probe the molecular mechanisms of high viscosity of an IgGmAbsArticle
- Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Preferential interactions of excipients with the antibody surface govern their effect on the stability of antibodies in solution. We probed the preferential interactions of proline, arginine.HCl (Arg.HCl), and NaCl with three therapeutically relevant IgG1 antibodies via experiment and simulation. With simulations, we examined how excipients interacted with different types of surface patches in the variable region (Fv). For example, proline interacted most strongly with aromatic surfaces, Arg.HCl was included near negative residues, and NaCl was excluded from negative residues and certain hydrophobic regions. The differences in interaction of different excipients with the same surface patch on an antibody may be responsible for variations in the antibody's aggregation, viscosity, and self-association behaviors in each excipient. Proline reduced self-association for all three antibodies and reduced aggregation for the antibody with an association-limited aggregation mechanism. The effects of Arg.HCl and NaCl on aggregation and viscosity were highly dependent on the surface charge distribution and the extent of exclusion from highly hydrophobic patches. At pH 5.5, both tended to increase the aggregation of an antibody with a strongly positive charge on the Fv, while only NaCl reduced the aggregation of the antibody with a large negative charge patch on the Fv. Arg.HCl reduced the viscosities of antibodies with either a hydrophobicity-driven mechanism or a charge-driven mechanism. Analysis of this data presents a framework for understanding how amino acid and ionic excipients interact with different protein surfaces, and how these interactions translate to the observed stability behavior.
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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.