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Related Experiment Videos

Selective protein adsorption on a phase-separated solvent-cast polymer blend.

Alioscka Sousa1, Merih Sengonul, Robert Latour

  • 1Department of Chemical, Biomedical, and Materials Engineering, Stevens Institute of Technology, Hoboken, New Jersey 07030, USA.

Langmuir : the ACS Journal of Surfaces and Colloids
|June 28, 2006
PubMed
Summary

Protein adsorption on polymer blends is influenced by surface morphology. Ferritin selectively adsorbs to specific polymer phases at physiological pH, but this selectivity is lost at lower pH, impacting biomedical device design.

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Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Polymer Science

Background:

  • Biomedical device sophistication relies on advanced polymer compositions like copolymers and blends.
  • Heterogeneous surface morphology in phase-separated polymers raises questions about protein adsorption.
  • Controlling protein adsorption is crucial for developing physiologically compatible surfaces.

Purpose of the Study:

  • To investigate the short-time adsorption of ferritin onto phase-separated polymer blends.
  • To understand the role of heterogeneous surface morphology in protein adsorption.
  • To explore the influence of pH on ferritin adsorption selectivity.

Main Methods:

  • Studied ferritin adsorption on polycaprolactone (PCL) and desaminotyrosyl-tyrosine dodecyl ester polycarbonate (PDTD) blends.

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  • Utilized transmission electron microscopy (TEM) and electron energy-loss spectroscopy (EELS) for morphology characterization.
  • Investigated adsorption at physiological and acidic pH.

    • Main Results:

    • Ferritin selectively adsorbed onto the PDTD phase at physiological pH (approx. 3x higher density than PCL).
    • Selective adsorption disappeared at pH below ferritin's isoelectric point, with density becoming phase-independent.
    • Attributed selectivity to electrostatic repulsion between negatively charged ferritin and PCL at physiological pH.

    Conclusions:

    • Polymer processing variables significantly influence film morphology and surface properties.
    • Surface morphology and phase separation critically affect short-time protein adsorption.
    • Findings highlight the importance of processing control for predictable protein interactions in biomedical devices.