Immobilization of streptavidin on 4H–SiC for biosensor development
[Display omitted] ► Demonstrated specific and selective protein attachment on the SiC surface. ► APTES-on-SiC thickness is critical for biotinylation and protein immobilization steps. ► Biotinylation of the SiC surface eliminates non-specific protein attachment. A sequential layer formation chemistr...
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Published in | Applied surface science Vol. 258; no. 16; pp. 6056 - 6063 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
01.06.2012
Elsevier |
Subjects | |
Online Access | Get full text |
ISSN | 0169-4332 1873-5584 |
DOI | 10.1016/j.apsusc.2012.02.137 |
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Summary: | [Display omitted]
► Demonstrated specific and selective protein attachment on the SiC surface. ► APTES-on-SiC thickness is critical for biotinylation and protein immobilization steps. ► Biotinylation of the SiC surface eliminates non-specific protein attachment.
A sequential layer formation chemistry is demonstrated for the functionalization of silicon carbide (SiC) appropriate to biosensing applications. (0001) 4H–SiC was functionalized with 3-aminopropyltriethoxysilane (APTES) and subsequently biotinylated for the selective immobilization of streptavidin. Atomic force microscopy, X-ray photoelectron spectroscopy, ellipsometry, fluorescence microscopy, and contact angle measurements were utilized to determine the structure, thickness, wettability, and reactivity of the resulting surface after each functionalization step. Optimization of the APTES layer was found to be critical to the success of the subsequent steps; multilayer, polymeric films resulted in irreproducible behavior. It was shown that there was significant non-specific (electrostatic) binding of streptavidin to APTES functionalized SiC, thus revealing the importance of a uniform biotinylation step prior to streptavidin attachment. The experimental results demonstrate that the APTES functionalized and biotinylated SiC surface has the potential to be employed as a biosensing platform for the selective detection of streptavidin molecules. |
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ISSN: | 0169-4332 1873-5584 |
DOI: | 10.1016/j.apsusc.2012.02.137 |