Adsorption of fibrinogen and lysozyme on silicon grafted with poly(2-methacryloyloxyethyl phosphorylcholine) via surface-initiated atom transfer radical polymerization
| Autor: | Kazuhiko Ishihara, Shiping Zhu, John L. Brash, Wei Feng |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Silicon
Phosphorylcholine chemistry.chemical_element Microscopy Atomic Force Contact angle chemistry.chemical_compound Adsorption X-ray photoelectron spectroscopy Polymethacrylic Acids immune system diseases Polymer chemistry Electrochemistry General Materials Science Spectroscopy Binding Sites Atom-transfer radical-polymerization Fibrinogen Water Surfaces and Interfaces Condensed Matter Physics Monomer chemistry Polymerization Methacrylates Indicators and Reagents Muramidase Lysozyme |
| Zdroj: | Langmuir : the ACS journal of surfaces and colloids. 21(13) |
| ISSN: | 0743-7463 |
| Popis: | Surfaces based on grafted poly(2-methacryloyloxyethyl phosphorylcholine) (poly(MPC)) "brushes" with a constant graft density of 0.39 chain/nm2 and chain length from 5 to 200 monomer units were prepared by surface-initiated atom transfer radical polymerization (ATRP) on silicon wafers. The chain length and layer thickness of the poly(MPC) grafts were varied via the ratio of MPC to sacrificial initiator. The surfaces were characterized by water contact angle, XPS, and AFM. The effect of poly(MPC) chain length on fibrinogen and lysozyme adsorption was studied in TBS buffer at pH 7.4. The adsorption of both proteins on the poly(MPC)-grafted surfaces was greatly reduced compared to the unmodified silicon. Adsorption decreased with increasing chain length of the poly(MPC) grafts. Grafts of chain length 200 (MW 59 000) gave adsorption levels of 7 and 2 ng/cm2, respectively, for fibrinogen and lysozyme at 1 mg/mL protein concentration, corresponding to reductions of greater than 98% compared to the unmodified silicon. Adsorption experiments using mixtures of the two proteins showed that the suppression of protein adsorption on the poly(MPC)-grafted surfaces was not strongly dependent on protein size or charge. |
| Databáze: | OpenAIRE |
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