A photoimmobilizable sulfobetaine-based polymer for a nonbiofouling surface
A novel photoreactive polymer containing sulfobetaine polar groups was prepared by copolymerization of two kinds of methacrylic acids with sulfobetaine and azidoaniline. The polymer was photoimmobilized on polyester and polystyrene surfaces. Its effects on surface modification were investigated from...
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Veröffentlicht in: | Materials Science & Engineering C 2010-01, Vol.30 (2), p.316-322 |
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Sprache: | eng |
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Zusammenfassung: | A novel photoreactive polymer containing sulfobetaine polar groups was prepared by copolymerization of two kinds of methacrylic acids with sulfobetaine and azidoaniline. The polymer was photoimmobilized on polyester and polystyrene surfaces. Its effects on surface modification were investigated from its interactions with water, proteins and cells. Polymer immobilization altered both of the plain surfaces to becoming hydrophilic in a similar range of static contact angles (12.5±1.6° on polyester and 14.7±2.2° on polystyrene). This suggests that the surfaces were covered with sulfobetaine polar groups. Micropattern immobilization was carried out on both polymers using a photomask. The formed pattern was identical to the photomask, showing that the polymer was formed in response to ultraviolet irradiation. Measurements using atomic force microscopy showed that the polymer was formed at a thickness of 550nm, demonstrating that the polymer was cross-linked with itself and with the substrate molecules. Measurements using time-of-flight secondary ion mass spectrometry detected an abundance of sulfur-containing ions in the patterned polymer, confirming that sulfobetaine had been immobilized. Protein adsorption and mammalian cell adhesiveness were reduced markedly on the immobilized regions. The reduction of cell adhesiveness was concentration-dependent for the immobilized polymer on polyester surfaces. In conclusion, a novel sulfobetaine-containing polymer was immobilized photoreactively on conventional polymer surfaces and significantly reduced interactions with proteins and mammalian cells. |
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ISSN: | 0928-4931 1873-0191 |
DOI: | 10.1016/j.msec.2009.11.006 |