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Polymer Classification: Stereospecificity01:26

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Preparation of Hollow Polystyrene Particles and Microcapsules by Radical Polymerization of Janus Droplets Consisting of Hydrocarbon and Fluorocarbon Oils
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Core (Polystyrene)-Shell [Poly(glycerol monomethacrylate)] Particles.

Andrew Mckenzie1, Richard Hoskins2, Thomas Swift2

  • 1Department of Chemistry, University of Sheffield , Sheffield, South Yorkshire S3 7HF, U.K.

ACS Applied Materials & Interfaces
|February 14, 2017
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Summary
This summary is machine-generated.

Synthesized core-shell particles resist protein adsorption. Particle shell formulation influences the degree of protein adsorption, offering tunable anti-fouling properties for advanced applications.

Keywords:
core−shellemulsion polymerizationhydrogelparticlesprotein adsorption

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Area of Science:

  • Materials Science
  • Polymer Chemistry
  • Surface Science

Background:

  • Core-shell particles are crucial in various applications, but their surface properties, particularly protein adsorption, require careful control.
  • Emulsion polymerization offers a versatile method for synthesizing tailored core-shell nanostructures.

Purpose of the Study:

  • To synthesize water-swollen core-shell particles with tunable shell properties.
  • To evaluate the protein adsorption resistance of these particles using common model proteins.
  • To investigate the impact of shell formulation on protein adsorption behavior.

Main Methods:

  • Emulsion polymerization of a 1,3-dioxolane functional monomer to create core-shell particles.
  • Hydrolysis to remove the 1,3-dioxolane group and induce shell swelling.
  • Bicinchoninic acid assay and ζ-potential measurements to quantify protein adsorption.
  • Systematic variation of cross-linking and shell monomer content in the feed.

Main Results:

  • Synthesized core-shell particles exhibited swelling in aqueous media, increasing size post-hydrolysis.
  • Core-shell particles demonstrated significantly reduced protein adsorption compared to uncoated polystyrene cores.
  • Protein adsorption levels varied based on the difunctional cross-linking and shell monomer concentrations used.
  • Adsorption of lysozyme, albumin, and fibrinogen was dependent on the specific shell formulation.

Conclusions:

  • The developed core-shell particles exhibit inherent resistance to protein adsorption.
  • Shell composition is a critical factor in controlling protein-repellent properties.
  • These findings suggest potential for designing advanced anti-fouling surfaces and drug delivery systems.