Bioactive Antifouling Surfaces by Visible-Light-Triggered Polymerization
| Autor: | Jacob Baggerman, Ai T. Nguyen, Andriy R. Kuzmyn, Han Zuilhof |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Materials science
nonfouling coatings Radical polymerization 02 engineering and technology 010402 general chemistry Methacrylate 01 natural sciences Biofouling controlled living polymerization Copolymer Fourier transform infrared spectroscopy VLAG chemistry.chemical_classification Mechanical Engineering Organic Chemistry Polymer 021001 nanoscience & nanotechnology Organische Chemie zwitterionic polymer brushes 0104 chemical sciences 3. Good health chemistry Chemical engineering Polymerization Mechanics of Materials Attenuated total reflection biosensing 0210 nano-technology |
| Zdroj: | Advanced Materials Interfaces, 6(12) Advanced Materials Interfaces Advanced Materials Interfaces 6 (2019) 12 |
| ISSN: | 2196-7350 |
| Popis: | Hierarchical bioactive surfaces are created by visible-light-induced surface-initiated living radical polymerization employing tris[2-phenylpyridinato-C2,N]iridium(III) as a photocatalyst. The hierarchical antifouling diblock copolymer structures consist of N-(2-hydroxypropyl)-methacrylamide (first block) and carboxybetaine methacrylate (second block). The living nature of the polymerization is shown by a linear increase in layer thickness (as measured by atomic force microscopy) and reinitiation of the polymerization to create a patterned second block of polymer. The chemical structure of the brushes is confirmed by X-ray photoelectron spectroscopy and attenuated total reflection Fourier transform infrared spectroscopy measurements. The block copolymer brushes demonstrate excellent antifouling properties when exposed to single-protein solutions or to bovine serum. The second carboxybetaine block of the hierarchical antifouling structures can effectively be biofunctionalized with an anti-fibrinogen antibody. The coated surfaces show a high affinity and specificity to fibrinogen, while preventing nonspecific adsorption from other proteins in bovine serum. |
| Databáze: | OpenAIRE |
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