- Tizazu, G. and el Zubir, O. and Patole, S. and McLaren, A. and Vasilev, C. and Mothersole, D. J. and Adawi, A. and Hunter, C. N. and Lidzey, D. G. and Lopez, G. P. and Leggett, G. J., Micrometer and Nanometer Scale Photopatterning of Proteins on Glass Surfaces by Photo-degradation of Films Formed from Oligo(Ethylene Glycol) Terminated Silanes,
Biointerphases, vol. 7 no. 1-4
(2012) [doi] .
(last updated on 2013/06/21)
Exposure of films formed by the adsorption of oligo(ethylene glycol) (OEG) functionalized trichlorosilanes on glass to UV light from a frequency-doubled argon ion laser (244 nm) causes photodegradation of the OEG chain. Although the rate of degradation is substantially slower than for monolayers of OEG terminated thiolates on gold, it is nevertheless possible to form micrometer-scale patterns by elective adsorption of streptavidin to exposed regions. A low density of aldehyde functional groups is produced, and this enables derivatization with nitrilotriacetic acid via an amine linker. Complexation with nickel enables the site-specific immobilization of histidine-tagged yellow and green fluorescent proteins. Nanometer-scale patterns may be fabricated using a Lloyd's mirror interferometer, with a sample and mirror set at right angles to each other. At low exposures, partial degradation of the OEG chains does not remove the protein-resistance of the surface, even though friction force microscopy reveals the formation of patterns. At an exposure of ca. 18 J cm(-2), the modified regions became adhesive to proteins in a narrow region ca. 30 nm (lambda/8) wide. As the exposure is increased further the lines quickly broaden to ca. 90 nm. Adjustment of the angle between the sample and mirror enables the fabrication of lines of His-tagged green fluorescent protein at a period of 340 nm that could be resolved using a confocal microscope.