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Controlled delivery systems for proteins using polyanhydride microspheres

Y Tabata1, S Gutta, R Langer

  • 1Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge 02139.

Pharmaceutical Research
|April 1, 1993
PubMed
Summary
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This study developed polyanhydride microspheres for sustained protein release, showing protected enzyme activity and near-constant drug delivery without initial bursts. The novel method ensures stable protein release from biodegradable drug delivery systems.

Area of Science:

  • Biomaterials Science
  • Drug Delivery Systems
  • Polymer Chemistry

Background:

  • High molecular weight, water-soluble proteins require advanced delivery systems for sustained therapeutic effects.
  • Polyanhydride microspheres offer potential for controlled drug release due to their biodegradability.
  • Challenges exist in maintaining protein stability and achieving consistent release kinetics from such matrices.

Purpose of the Study:

  • To develop and characterize polyanhydride microspheres for near-constant sustained release of high molecular weight proteins.
  • To evaluate the protective effect of microspheres on enzyme activity.
  • To investigate the release kinetics and degradation mechanisms of protein-loaded polyanhydride microspheres.

Main Methods:

  • Proteins (lysozyme, trypsin, heparinase, ovalbumin, albumin, immunoglobulin) were encapsulated into poly(fatty acid dimer) (PFAD), poly(sebacic acid) (PSA), and their copolymers [P(FAD-SA)] microspheres using a double emulsion solvent evaporation method.

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  • Microsphere characteristics (size, encapsulation efficiency) were analyzed.
  • Enzymatic activity, release profiles, degradation kinetics (monomer release), and protein-matrix interactions (DSC) were studied.

    • Main Results:

    • Spherical P(FAD-SA) microspheres (50-125 microns) achieved >80% protein encapsulation efficiency, irrespective of protein size.
    • Encapsulation protected enzymes; trypsin and heparinase showed significantly reduced activity loss compared to free enzymes.
    • Microspheres exhibited near-zero-order erosion kinetics over 5 days, with sustained protein release without an initial burst, continuing even after matrix degradation.

    Conclusions:

    • Polyanhydride microspheres provide an effective platform for sustained, controlled release of high molecular weight proteins.
    • Protein interaction with degradation monomers (FAD) likely forms insoluble aggregates, enabling delayed release.
    • Minimizing sonication during preparation is crucial to preserve protein activity, reducing loss to ~20%.