Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Review: Why is arginine effective in suppressing aggregation?

Kohei Tsumoto1, Daisuke Ejima, Yoshiko Kita

  • 1Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Sendai, Japan.

Protein and Peptide Letters
|March 9, 2006
PubMed
Summary

Arginine effectively suppresses protein aggregation and weakens protein-protein interactions, aiding in protein production and purification. It acts as an aggregation suppressor, not a protein stabilizer, with unique mechanisms distinct from strong denaturants.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Tryptophan-Mediated Sodium Dodecyl Sulfate Binding to Proteins.

The protein journal·2026
Same author

Editorial for Special Issue "Recombinant Proteins for Molecular Biology Research: Technologies and Applications".

Current issues in molecular biology·2026
Same author

Design of Analytical Methods for Protein Adsorption Characteristics at Material Interfaces.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

Process-analytical study of IL-6 refolding during batch buffer exchange.

European biophysics journal : EBJ·2026
Same author

Parameter optimization for circular dichroism spectroscopy of proteins: A practical approach for rapid acquisition of high-quality spectra.

Analytical biochemistry·2026
Same author

A robust and sensitive method for detecting subtle structural differences in bovine serum albumin.

BioTechniques·2026

Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Chemical Engineering

Background:

  • Arginine is widely used in protein production for refolding and improving yields.
  • Its role in suppressing aggregation and facilitating protein purification, like antibody elution via Protein-A chromatography, is recognized.
  • Observed effects suggest arginine weakens protein-protein interactions, but the underlying mechanism remains unclear.

Purpose of the Study:

  • To investigate the mechanism by which arginine reduces protein-protein interactions and suppresses protein aggregation.
  • To clarify whether arginine acts as a protein stabilizer or an aggregation suppressor.
  • To differentiate the aggregation-suppressing effects of arginine from those of strong denaturants.

Main Methods:

  • Examined the effects of arginine on the stability and solubility of pure proteins.

Related Experiment Videos

  • Compared the action of arginine with strong denaturants known to suppress aggregation.

    • Main Results:

    • Arginine was found to be an aggregation suppressor, not a protein stabilizer.
    • Arginine effectively weakens protein-protein interactions, aiding in protein solubilization and elution.
    • The study highlights unique aspects of arginine's function in protein processing.

    Conclusions:

    • Arginine's primary role in protein processing is aggregation suppression, achieved by weakening protein-protein interactions.
    • The mechanism of arginine's aggregation suppression differs from that of strong denaturants.
    • Understanding these mechanisms can optimize protein production and purification strategies.