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Polyphosphazene (PCPP) adjuvants self-assemble with model antigens like lysozyme, forming complexes with high protein loading. Complexation regimes and antigenicity depend on salt concentration and mixing order.

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Area of Science:

  • Polymer Chemistry
  • Immunology
  • Materials Science

Background:

  • Polyphosphazenes are flexible polyelectrolytes with immunoadjuvant properties.
  • Their adjuvant activity relies on non-covalent self-assembly with antigenic proteins via charge complexation.

Purpose of the Study:

  • To investigate the self-assembly of poly[di(carboxylatophenoxy)phosphazene] (PCPP) with hen egg lysozyme.
  • To characterize the resulting supramolecular complexes under physiological conditions.

Main Methods:

  • Automated dynamic light scattering titration
  • Asymmetric flow field flow fractionation (AF4)
  • Enzyme-linked immunosorbent assay (ELISA)
  • Fluorescent quenching

Main Results:

  • Three self-assembly regimes observed: nano-scale complexes, multi-chain complexes, and larger aggregates.
  • Maximum loading exceeded 600 protein molecules per PCPP chain; dissociation constant (Kd) in the micromolar range (7 × 10⁻⁶ mol/L).
  • Antigenicity retained in smaller complexes, reduced in heavily aggregated systems.

Conclusions:

  • Complexation is controllable via salt concentration (NaCl/KCl), showing ion-specific effects.
  • Higher NaCl concentrations favored smaller complexes, contrary to solubility predictions.
  • Order of mixing significantly impacts complexation at low stoichiometries, an effect diminished by high salt concentrations.