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Energetic Dissection of Mab-Specific Reversible Self-Association Reveals Unique Thermodynamic Signatures.

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Summary

Reversible self-association (RSA) in therapeutic monoclonal antibodies (mAbs) was studied. Monoclonal antibody C exhibits enthalpically-driven isodesmic self-association, while monoclonal antibody E shows entropically-driven monomer-dimer self-association.

Keywords:
analytical ultracentrifugationdynamic light scatteringinteracting systemsmonoclonal antibodynonidealitysedimentation velocity

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Area of Science:

  • Biochemistry
  • Protein aggregation
  • Therapeutic antibodies

Background:

  • Reversible self-association (RSA) poses challenges in developing therapeutic monoclonal antibodies (mAbs).
  • Previous analysis identified significant RSA in five IgG mAbs under matched conditions.
  • Understanding the thermodynamic mechanisms of RSA is crucial for antibody development.

Purpose of the Study:

  • To investigate the thermodynamics of RSA for two specific mAbs (C and E) exhibiting strong RSA.
  • To elucidate the underlying mechanisms driving RSA in these selected mAbs.
  • To provide insights into the energetics of antibody self-association.

Main Methods:

  • Utilized concentration-dependent dynamic light scattering and sedimentation velocity (SV) studies.
  • Performed SV analyses over a range of temperatures to capture thermodynamic changes.
  • Employed global analysis with direct boundary fitting to accurately determine interaction energetics, accounting for nonideality.

Main Results:

  • Monoclonal antibody C demonstrated isodesmic self-association across all tested temperatures.
  • The energetics for mAb C indicated an enthalpically-driven process with a significant entropic penalty.
  • Monoclonal antibody E displayed monomer-dimer self-association, primarily driven by entropy with minimal enthalpic contribution.

Conclusions:

  • Classical interpretations suggest van der Waals/H-bond interactions for mAb C and electrostatic interactions for mAb E.
  • Acknowledged the potential coupling of RSA to other equilibria.
  • Highlighted the limitations of current interpretations in fully explaining RSA mechanisms.