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Related Experiment Videos

Interactions among proteins and hydrophobically modified polyelectrolytes.

L E Bromberg1

  • 1Department of Physics and Center for Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge 02139, USA. cpbrolev@yahoo.com

The Journal of Pharmacy and Pharmacology
|May 9, 2001
PubMed
Summary

Hydrophobically modified poly(acrylic acid) (PAA) copolymers with Pluronic F127 NF form gels at body temperature, enhancing retention and stabilizing proteins like insulin. These Pluronic-PAA gels inhibit protein aggregation and degradation by enzymes.

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Area of Science:

  • Polymer Chemistry
  • Biomaterials Science
  • Drug Delivery

Background:

  • Hydrophobically modified polyelectrolytes offer unique properties for advanced applications.
  • Pluronic block copolymers are widely used in biomedical fields.
  • Protein stabilization and controlled release are critical in pharmaceutical development.

Purpose of the Study:

  • To synthesize and characterize Pluronic-PAA copolymers.
  • To investigate the gelation properties of Pluronic-PAA solutions at body temperature.
  • To evaluate the potential of Pluronic-PAA gels for protein stabilization and protection against degradation.

Main Methods:

  • Synthesis of poly(acrylic acid) conjugated with Pluronic F127 NF surfactant.
  • Rheological measurements to assess gelation behavior.

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  • Circular dichroism spectroscopy to study protein tertiary structures.
  • Shaking tests to evaluate protein aggregation.
  • Enzymatic degradation assays using alpha-chymotrypsin and trypsin.

    • Main Results:

    • Pluronic-PAA copolymer solutions formed gels at low concentrations and body temperature.
    • Gelled solutions demonstrated enhanced retention properties.
    • Tertiary structures of human insulin, hemoglobin, and albumin were stabilized.
    • Insulin aggregation was impeded in Pluronic-PAA gels.
    • Pluronic-PAA significantly hindered insulin degradation by alpha-chymotrypsin (7-fold).
    • Pluronic-PAA inhibited trypsin activity by extracting calcium ions, preventing protein degradation.

    Conclusions:

    • Pluronic-PAA copolymers form thermoreversible gels with potential for topical applications.
    • These gels effectively stabilize protein structures and prevent aggregation.
    • Pluronic-PAA acts as a protective agent against enzymatic degradation of proteins, offering a novel approach for protein stabilization.