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Polymorphism refers to the existence of a drug substance in multiple crystalline forms, known as polymorphs. Recently, this term has been expanded to include solvates (forms containing a solvent), amorphous forms (non-crystalline forms), and desolvated solvates (forms from which the solvent has been removed).
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Area of Science:

  • Biophysics
  • Materials Science
  • Pharmacology

Background:

  • Exogenous pulmonary surfactants (EPS) are promising for drug delivery to the lungs.
  • Polymyxin B (PxB) is an antibiotic with potential for combined therapy when delivered via EPS.
  • Understanding PxB interaction with EPS is crucial for optimizing drug delivery strategies.

Purpose of the Study:

  • To evaluate the interaction between polymyxin B (PxB) and poractant alfa Curosurf (PSUR), a clinically used EPS.
  • To compare PxB interaction with PSUR and a protein-free model system (MS) to understand composition-specific effects.
  • To determine the impact of PxB binding on the structural and physical properties of PSUR.

Main Methods:

  • Differential scanning calorimetry (DSC)
  • Small- and wide-angle X-ray scattering (SAXS/WAXS)
  • Small-angle neutron scattering (SANS)
  • Fluorescence spectroscopy
  • Electrophoretic light scattering (ELS)

Main Results:

  • Electrostatic interactions dominate PxB binding to EPS, with PxB localizing on the PSUR bilayer surface.
  • PxB binding strengthens the multilamellar structure of PSUR and negligibly affects lipid bilayer thickness.
  • PxB does not alter PSUR's gel-to-fluid phase transition temperature, but increases it in the protein-free MS.

Conclusions:

  • The study supports the concept of combined therapy using PxB-enriched Curosurf for lung drug delivery.
  • PxB's hydrophobic tail does not penetrate the lipid bilayer, and its binding strengthens the surfactant structure.
  • Careful assessment of PxB concentration ( < 5 wt %) is recommended to prevent surface charge inversion.