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Stress-dependent interfacial competition with direct binding enhances IgG4 stabilization.

Yan Gao1, Hengqian Wu2, Lili Wang2

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This study reveals how polysorbates and poloxamer 188 stabilize immunoglobulin G4 (IgG4) monoclonal antibodies (mAbs) under different stresses. Their effectiveness depends on stress type and surfactant concentration relative to critical micelle concentration (CMC).

Keywords:
AggregationCritical micelle concentration (CMC)IgG4Poloxamer 188Polysorbates

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Area of Science:

  • Biochemistry
  • Materials Science
  • Pharmaceutical Sciences

Background:

  • Immunoglobulin G4 (IgG4) monoclonal antibodies (mAbs) are crucial therapeutics but possess unique structural vulnerabilities.
  • Nonionic surfactants like polysorbates (Tween 20/80) and poloxamer 188 (P188) are commonly used to stabilize protein formulations.
  • Understanding the mechanisms by which these surfactants protect IgG4 mAbs under various stress conditions is essential for rational formulation design.

Purpose of the Study:

  • To elucidate the stress-dependent stabilization mechanisms of polysorbates and poloxamer 188 for IgG4 mAbs.
  • To investigate the role of protein-surfactant interactions, critical micelle concentration (CMC), and adsorption kinetics in stabilization.
  • To establish a framework connecting fundamental interactions to formulation strategies for IgG4 mAbs.

Main Methods:

  • Utilized isothermal titration calorimetry (ITC) to study protein-surfactant binding thermodynamics.
  • Measured critical micelle concentration (CMC) to understand surfactant aggregation behavior.
  • Employed a multi-stress model including orbital shaking, vortex stress, and freeze-thaw cycles to assess stabilization efficacy.
  • Investigated stabilization mechanisms under both thermodynamically and kinetically controlled stress conditions.

Main Results:

  • Polysorbates interact with IgG4 via entropy-driven hydrophobic interactions, while P188 does not show significant binding.
  • Both surfactants stabilize IgG4 at concentrations above their CMC through interfacial adsorption under mild stress.
  • Under intense vortex stress, polysorbates require supra-CMC concentrations for full protection, acting as monomer reservoirs, whereas P188 offers limited stabilization due to slower adsorption kinetics.
  • Stabilization mechanisms are distinct and depend on the type and intensity of the applied stress.

Conclusions:

  • IgG4 stabilization by nonionic surfactants is governed by distinct, stress-dependent pathways.
  • Polysorbates and P188 exhibit different stabilization mechanisms based on their interaction profiles and adsorption kinetics.
  • The findings facilitate a shift from empirical screening to mechanism-guided selection of stabilizers for IgG4 mAb formulations, improving drug product stability and efficacy.