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Single-Molecule Dynamics Reflect IgG Conformational Changes Associated with Ion-Exchange Chromatography.

Anastasiia Misiura1, Hao Shen2, Lawrence Tauzin1

  • 1Department of Chemistry, Rice University, 6100 Main Street, Houston, Texas 77005, United States.

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Antibody unfolding during ion-exchange chromatography (IEX) is influenced by salt conditions. Lower salt concentrations promote unfolding and alter protein motion, impacting elution profiles in pharmaceutical separations.

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Area of Science:

  • Biochemistry
  • Chromatography
  • Protein Science

Background:

  • Conformational changes in biologics like antibodies can compromise pharmaceutical separation efficiency.
  • Understanding antibody-stationary phase interactions in ion-exchange chromatography (IEX) is crucial for optimizing these processes.

Purpose of the Study:

  • To investigate the impact of conformational changes on antibody motion and elution profiles during IEX.
  • To elucidate the mechanistic details of antibody-stationary phase interactions under varying salt conditions.

Main Methods:

  • Utilized ion-exchange chromatography (IEX) coupled with three-dimensional single-protein tracking.
  • Employed circular dichroism spectroscopy to monitor conformational changes in a model antibody (immunoglobulin G, IgG).

Main Results:

  • Absence of salt enhanced electrostatic attraction between IgG and the stationary phase.
  • Low salt conditions promoted surface-induced unfolding of IgG, slowing protein motion.
  • Altered IgG motion and unfolding significantly decreased elution from the IEX column.

Conclusions:

  • Revealed previously unreported details of antibody structural changes during IEX.
  • Demonstrated how IgG conformational alterations influence macroscale elution profiles.
  • Provided critical insights into antibody-stationary phase interactions for improved pharmaceutical separations.