Journal
LANGMUIR
Volume 33, Issue 35, Pages 8829-8837Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.langmuir.7b01255
Keywords
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Funding
- EPSRC [EP/I012060/1]
- Biotechnology and Biological Sciences Research Council (BBSRC UK) [BB/M000265/1]
- European Research Council [338895]
- Photosynthetic Antenna Research Center (PARC)
- Energy Frontier Research Center - U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-SC 0001035]
- Biotechnology and Biological Sciences Research Council [BB/M000265/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/I012060/1] Funding Source: researchfish
- BBSRC [BB/M000265/1] Funding Source: UKRI
- EPSRC [EP/I012060/1] Funding Source: UKRI
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We show that sequential protein deposition is possible by photodeprotection of films formed from a tetraethylene-glycol functionalized nitrophenylethoxycarbonyl-protected aminopropyltriethoxysilane (NPEOC-APTES). Exposure to near-UVirradiation removes the protein-resistant protecting group, and allows protein adsorption onto the resulting aminated surface. The protein resistance was tested using proteins with fluorescent labels and microspectroscopy of two-component structures formed by micro-and nano patterning and deposition of yellow and green fluorescent proteins (YFP/GFP). Nonspecific adsorption onto regions where the protecting group remained intact was negligible. Multiple component patterns were also formed by near-field methods. Because reading and writing can be decoupled in a near-field microscope, it is possible to carry out sequential patterning steps at a single location involving different proteins. Up to four different proteins were formed into geometric patterns using near-field lithography. Interferometric lithography facilitates the organization of proteins over square cm areas. Two-component patterns consisting of 150 nm streptavidin dots formed within an orthogonal grid of bars of GFP at a period of ca. 500 nm could just be resolved by fluorescence microscopy.
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