ArticlePloS one2013
Arginine inhibits adsorption of proteins on polystyrene surface.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 33 citations in OpenAlex.
- Comparative evaluation of four immunoassays for Plasmodium vivax serological detection using recombinant PvMSP1-42 antigen.PLoS neglected tropical diseases · 2026Article
- Effects of arginine in therapeutic protein formulations: a decade review and perspectives.Antibody therapeutics · 2023Review
- Differences in interaction lead to the formation of different types of insulin amyloid.Scientific reports · 2022Article
- A Robust Method for Assaying the Immunoreactive Fraction in Nonequilibrium Systems.Pharmaceuticals (Basel, Switzerland) · 2019Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nonspecific adsorption of protein on solid surfaces causes a reduction of concentration as well as enzyme inactivation during purification and storage. However, there are no versatile inhibitors of the adsorption between proteins and solid surfaces at low concentrations. Therefore, we examined additives for the prevention of protein adsorption on polystyrene particles (PS particles) as a commonly-used material for vessels such as disposable test tubes and microtubes. A protein solution was mixed with PS particles, and then adsorption of protein was monitored by the concentration and activity of protein in the supernatant after centrifugation. Five different proteins bound to PS particles through electrostatic, hydrophobic, and aromatic interactions, causing a decrease in protein concentration and loss of enzyme activity in the supernatant. Among the additives, including arginine hydrochloride (Arg), lysine hydrochloride, guanidine hydrochloride, NaCl, glycine, and glucose, Arg was most effective in preventing the binding of proteins to PS particles as well as activity loss. Moreover, even after the mixing of protein and PS particles, the addition of Arg caused desorption of the bound protein from PS particles. This study demonstrated a new function of Arg, which expands the potential for application of Arg to proteins.
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