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Non-specific and specific interactions on functionalized polymer surface studied by FT-SPR.

Jizheng Wei1, Lesan Yan, Xiuli Hu

  • 1State Key Laboratory of Polymer Physics and Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, 5625 Renmin Street, Changchun 130022, PR China.

Colloids and Surfaces. B, Biointerfaces
|December 15, 2010
PubMed
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Fourier transform surface plasmon resonance (FT-SPR) effectively studied protein interactions with a biotinylated polymer film. Surface treatments influenced streptavidin and bovine serum albumin adsorption, highlighting specific biotin-streptavidin binding.

Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Analytical Chemistry

Background:

  • Developing functional polymer surfaces is crucial for biosensor applications.
  • Understanding protein-surface interactions is key to controlling biomolecule adsorption.
  • Biotinylated polymers offer specific binding sites for streptavidin.

Purpose of the Study:

  • To investigate protein adsorption on a biotinylated polymer film using FT-SPR.
  • To analyze specific and non-specific interactions of streptavidin and bovine serum albumin.
  • To evaluate the impact of surface modifications on protein binding.

Main Methods:

  • Synthesis of poly(lactide-co-2,2-dihydroxymethyl-propylene carbonate-graft-biotin) [P(LA-co-DHC/biotin)] via ring-opening copolymerization and biotinylation.

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  • Coating the polymer onto an FT-SPR chip and applying different surface treatments (vacuum-drying, hydration, blocking).
  • Monitoring protein adsorption (streptavidin and BSA) using Fourier transform surface plasmon resonance (FT-SPR).

    • Main Results:

    • Vacuum-dried films showed the highest BSA adsorption.
    • Hydration treatment reduced BSA adsorption by exposing biotin moieties.
    • Blocking agents saturated surface sites, decreasing both BSA and streptavidin adsorption.
    • Streptavidin exhibited enhanced adsorption compared to BSA due to specific biotin-streptavidin interactions, particularly on blocked surfaces.

    Conclusions:

    • FT-SPR is a suitable technique for studying polymer-biomolecule interactions.
    • Surface treatments significantly modulate protein adsorption behavior on biotinylated polymer films.
    • Specific interactions (biotin-streptavidin) can be distinguished from non-specific adsorption (BSA) using this method.