ArticlePharmaceutical research2014
Thermodynamic and fluorescence analyses to determine mechanisms of IgG1 stabilization and destabilization by arginine.
Article in Pharmaceutical research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 62 citations in OpenAlex.
- Article
- Bayesian Optimization for Efficient Multiobjective Formulation Development of Biologics.Molecular pharmaceutics · 2025Article
- Exploring the Potential of Arginine to Increase Coelenterazine-Renilla Luciferase Affinity and Enzyme Stability: Kinetic and Molecular Dynamics Studies.The protein journal · 2024Article
- Effects of arginine in therapeutic protein formulations: a decade review and perspectives.Antibody therapeutics · 2023Review
- The influence of excipients on the viscosity of monoclonal antibody solutions.Journal of molecular liquids · 2022Article
- Arginine and Arginine-Rich Peptides as Modulators of Protein Aggregation and Cytotoxicity Associated With Alzheimer's Disease.Frontiers in molecular neuroscience · 2021Review
- Viscosity Control of Protein Solution by Small Solutes: A Review.Current protein & peptide science · 2018Review
- Bilateral Effects of Excipients on Protein Stability: Preferential Interaction Type of Excipient and Surface Aromatic Hydrophobicity of Protein.Pharmaceutical research · 2017Article
- A change in the aggregation pathway of bovine serum albumin in the presence of arginine and its derivatives.Scientific reports · 2017Article
- Quantitative Correlation between Viscosity of Concentrated MAb Solutions and Particle Size Parameters Obtained from Small-Angle X-ray Scattering.Pharmaceutical research · 2015Article
- Advanced protein formulations.Protein science : a publication of the Protein Society · 2015Review
- The effect of arginine glutamate on the stability of monoclonal antibodies in solution.International journal of pharmaceutics · 2014Article
- Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeTo investigate mechanisms governing the stabilization and destabilization of immunoglobulin (IgG1) by arginine (Arg).
methodsThe effects of Arg on the aggregation/degradation, thermodynamic stability, hydrophobicity, and aromatic residues of IgG1 were respectively investigated by size-exclusion chromatography, differential scanning calorimetry, probe fluorescence, and intrinsic fluorescence.
resultsArg monohydrochloride (Arg-HCl) suppressed IgG1 aggregation at near-neutral pH, but facilitated aggregation and degradation at acidic pH or at high storage temperature. Equimolar mixtures of Arg and aspartic acid (Asp) or glutamic acid (Glu) suppressed aggregation without facilitating degradation even at high temperature. Arg-HCl decreased the thermodynamic stability of IgG1 by enthalpic loss, which was counteracted by using Asp or Glu as a counterion for Arg. The suppression of aggregation by Arg-HCl was well correlated with the decrease in hydrophobicity of IgG1. The intrinsic fluorescence of IgG1 was unaffected by Arg-HCl.
conclusionsSuppression of IgG1 aggregation can be attributed to the interaction between Arg and hydrophobic residues; on the other hand, facilitation of aggregation and degradation is presumably due to the interaction between Arg and some acidic residues, which could be competitively inhibited by simultaneously adding either Asp or Glu.
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