ArticleThe journal of physical chemistry. B2011
Arginine and the Hofmeister Series: the role of ion-ion interactions in protein aggregation suppression.
Article in The journal of physical chemistry. B, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 156 citations in OpenAlex.
- Article
- Stabilization of Bone Morphogenetic Protein-2 at Physiological pH: Contrasting Roles of CHAPS and Arginine in Aggregation Inhibition.Proteins · 2026Article
- Impact of Amino Acid Excipients on icIEF Method Development in Protein Therapeutics: A Formulation-Aware Analytical Framework.AAPS PharmSciTech · 2026Article
- Article
- Competitive adsorption of a monoclonal antibody and amphiphilic polymers to the air-water interface.European biophysics journal : EBJ · 2025Article
- The Thermodynamic and Gelation Properties of Ovalbumin and Lysozyme.Gels (Basel, Switzerland) · 2025Article
- Highly selective split intein method for efficient separation and purification of recombinant therapeutic proteins from mammalian cell culture fluid.Journal of chromatography. A · 2024Article
- Investigating Anion Effects on Metal Ion Binding Interactions With Amyloid β Peptide by Ion Mobility Mass Spectrometry.Journal of mass spectrometry : JMS · 2024Article
- Exploring the Potential of Arginine to Increase Coelenterazine-Renilla Luciferase Affinity and Enzyme Stability: Kinetic and Molecular Dynamics Studies.The protein journal · 2024Article
- The substrate-binding domains of the osmoregulatory ABC importer OpuA transiently interact.eLife · 2024Article
- SNSP113 (PAAG) improves mucociliary transport and lung pathology in the Scnn1b-Tg murine model of CF lung disease.Journal of cystic fibrosis : official journal of the European Cystic Fibrosis Society · 2023Article
- The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions.International journal of molecular sciences · 2023Article
- Host-Guest Complexation by β-Cyclodextrin Enhances the Solubility of an Esterified Protein.Molecular pharmaceutics · 2022Article
- Phase-specific RNA accumulation and duplex thermodynamics in multiphase coacervate models for membraneless organelles.Nature chemistry · 2022Article
- Modified Stability of microRNA-Loaded Nanoparticles.Pharmaceutics · 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
- Arginine and Arginine-Rich Peptides as Modulators of Protein Aggregation and Cytotoxicity Associated With Alzheimer's Disease.Frontiers in molecular neuroscience · 2021Review
- The Role of Counter-Ions in Peptides-An Overview.Pharmaceuticals (Basel, Switzerland) · 2020Review
- Divalent cations promote TALE DNA-binding specificity.Nucleic acids research · 2020Article
- Lysine-based dendrimer with double arginine residues.RSC advances · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
L-Arginine hydrochloride is a very important aggregation suppressor for which there has been much attention given regarding elucidating its mechanism of action. Little consideration, however, has been given toward other salt forms besides chloride, even though the counterion likely imparts a large influence per the Hofmeister Series. Here, we report an in depth analysis of the role the counterion plays in the aggregation suppression behavior of arginine. Consistent with the empirical Hofmeister series, we found that the aggregation suppression ability of other arginine salt forms on a model protein (α-chymotrypsinogen) follows the order: H(2)PO(4)(-) > SO(4)(2-) > citrate(2-) > acetate(-) ≈ F(-) ≈ Cl(-) > Br(-) > I(-) ≈ SCN(-). Mechanistically, preferential interaction and osmotic virial coefficient measurements, in addition to molecular dynamics simulations, indicate that attractive ion-ion interactions, particularly attractive interactions between arginine molecules, play a dominate role in the observed behavior. Furthermore, it appears that dihydrogen phosphate, sulfate, and citrate have strong attractive interactions with the guanidinium group of arginine, which seems to contribute to the superior aggregation suppression ability of those salt forms by bridging together multiple arginine molecules into clusters. These results not only further our understanding of how arginine influences protein stability, they also help to elucidate the mechanism behind the Hofmeister Series. This should help to improve biopharmaceutical stabilization through the use of other arginine salts and possibly, the development of novel excipients.
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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.