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IgG Charge: Practical and Biological Implications.

Danlin Yang1,2, Rachel Kroe-Barrett3, Sanjaya Singh4,5

  • 1Biotherapeutics Discovery Research, Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, CT 06877, USA. dyang55@its.jnj.com.

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PubMed
Summary
This summary is machine-generated.

Immunoglobulin G (IgG) charge significantly impacts solubility and biological function. Measured charges deviate from calculated values, highlighting the need for accurate charge assessment in therapeutic antibody selection.

Keywords:
IgG subclassesanalytical electrophoresismonoclonal IgGprotein chargeprotein–protein interactions

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Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Immunology

Background:

  • Immunoglobulin G (IgG) charge is a fundamental property influencing thermodynamic nonideality, solubility, and viscosity.
  • Biological activity, including clearance and potency, can vary between IgG charge isomers.
  • Previous understanding of IgG charge in physiological solvents was limited, lacking systematic exploration.

Purpose of the Study:

  • To systematically measure and characterize the charge of intact monoclonal antibody (mAb) IgGs and their fragments.
  • To compare measured IgG charges with calculated values based on H+ binding.
  • To establish guidelines for selecting therapeutic mAbs with optimal physiological properties based on charge.

Main Methods:

  • Membrane confined electrophoresis was used to measure the charge of twelve mAb IgGs and their F(ab')2 and Fc fragments.
  • Measurements were conducted in two solvents: pH 5.0 and phosphate-buffered saline (PBS) at pH 7.4.
  • A thermodynamically rigorous, concentration-dependent protein-protein interaction parameter was introduced.

Main Results:

  • Measured IgG charges significantly differed from calculated values at both pH 5.0 and pH 7.4.
  • Intact IgG charge depended on both Fv and Fc sequences but not as a simple sum of fragment charges.
  • IgG Fc fragment charges were consistent within classes, while intact IgG charges varied widely, with some outside the physiological range.
  • F(ab')2 fragments were nearly neutral for IgG1/IgG2 and anionic for some IgG4s at pH 7.4.

Conclusions:

  • Calculated charge based on H+ binding is insufficient for predicting actual IgG charge.
  • Accurate charge measurement is crucial for understanding IgG behavior and selecting therapeutic candidates.
  • Therapeutic mAbs should possess measured charges within the physiological range of serum-derived human IgGs for optimal performance.