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Biosurfaces Fabricated by Polymerization-Induced Surface Self-Assembly.

Wen Zhong1, Wangmeng Hou1, Yingze Liu1

  • 1Key Laboratory of Functional Polymer Materials, Ministry of Education, College of Chemistry, Nankai University, Collaborative Innovation Center of Chemical Science and Engineering, Tianjin 300071, China.

Langmuir : the ACS Journal of Surfaces and Colloids
|October 19, 2020
PubMed
Summary
This summary is machine-generated.

Polymerization-induced surface self-assembly (PISSA) enables fabrication of functional biosurfaces. This method preserves biomolecule activity, offering tunable protein immobilization for applications in drug delivery and tissue engineering.

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Area of Science:

  • Materials Science
  • Biotechnology
  • Polymer Chemistry

Background:

  • Surface biofunctionalization is crucial for advanced biological and clinical applications.
  • Synthesizing functional biosurfaces without damaging biomolecules presents a significant challenge.
  • Polymerization-induced surface self-assembly (PISSA) offers a promising route for creating tailored nanostructured surfaces.

Purpose of the Study:

  • To investigate the application of PISSA for fabricating robust biosurfaces.
  • To explore the synthesis of protein-functionalized polymer layers using controlled polymerization techniques.
  • To assess the structural integrity and activity of immobilized biomolecules during the PISSA process.

Main Methods:

  • Reversible addition-fragmentation chain transfer (RAFT) dispersion polymerization of N-isopropylacrylamide (NIPAM) using silica particle-bound and protein-bound RAFT agents.
  • Utilizing transmission electron microscopy (TEM) to analyze layer thickness and morphology.
  • Conducting kinetic studies to understand polymerization dynamics and self-assembly behavior.
  • Assessing the secondary structure and activity of immobilized bovine serum albumin (BSA) before and after cross-linking.

Main Results:

  • PNIPAM layers with BSA on top were successfully fabricated on silica particles via PISSA.
  • TEM confirmed that PNIPAM layer thickness correlates with monomer conversion.
  • Kinetic analysis revealed a critical point for surface coassembly of polymer brushes and protein bioconjugates.
  • Immobilized BSA retained its secondary structure and activity, exhibiting reversible "on-off" switching properties based on temperature-induced PNIPAM hydrophobicity.

Conclusions:

  • PISSA is an effective method for creating functional biosurfaces with preserved biomolecule activity.
  • The developed technique allows for tunable immobilization and stimuli-responsive behavior of proteins.
  • This approach holds potential for diverse applications including enzyme immobilization, drug delivery, and tissue engineering.