Enzyme-encapsulated silica monolayers for rapid functionalization of a gold surface
| Autor: | Shankar Balasubramanian, Glenn R. Johnson, Heather R. Luckarift, Sheetal Paliwal, Aleksandr Simonian |
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| Rok vydání: | 2007 |
| Předmět: |
Immobilized enzyme
Silicon dioxide education Nanoparticle Capsules chemistry.chemical_compound Colloid and Surface Chemistry Monolayer Organic chemistry Physical and Theoretical Chemistry Surface plasmon resonance Aryldialkylphosphatase Chemistry Self-assembled monolayer Surfaces and Interfaces General Medicine Surface Plasmon Resonance respiratory system DNA separation by silica adsorption Enzymes Immobilized Silicon Dioxide Chemical engineering Microscopy Electron Scanning Nanoparticles Surface modification Muramidase Gold Biotechnology |
| Zdroj: | Colloids and Surfaces B: Biointerfaces. 58:28-33 |
| ISSN: | 0927-7765 |
| DOI: | 10.1016/j.colsurfb.2006.08.013 |
| Popis: | We report a simple and rapid method for the deposition of amorphous silica onto a gold surface. The method is based on the ability of lysozyme to mediate the formation of silica nanoparticles. A monolayer of lysozyme is deposited via non-specific binding to gold. The lysozyme then mediates the self-assembled formation of a silica monolayer. The silica formation described herein occurs on a surface plasmon resonance (SPR) gold surface and is characterized by SPR spectroscopy. The silica layer significantly increases the surface area compared to the gold substrate and is directly compatible with a detection system. The maximum surface concentration of lysozyme was found to be a monolayer of 2.6 ng/mm(2) which allowed the deposition of a silica layer of a further 2 ng/mm(2). For additional surface functionalization, the silica was also demonstrated to be a suitable matrix for immobilization of biomolecules. The encapsulation of organophosphate hydrolase (OPH) was demonstrated as a model system. The silica forms at ambient conditions in a reaction that allows the encapsulation of enzymes directly during silica formation. OPH was successfully encapsulated within the silica particles and a detection limit for the substrate, paraoxon, using the surface-encapsulated enzyme was found to be 20 microM. |
| Databáze: | OpenAIRE |
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