Inducible site-selective bottom-up assembly of virus-derived nanotube arrays on RNA-equipped wafers
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chair:
Mueller, A. / Eber, F. / Azucena, C. / Petershans, A. / Bittner, A. / Gliemann, H. / Jeske, H. / Wege, C. (2011)
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place:
ACS Nano 5 (2011), 4512
- Date: 2011
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Mueller, A. / Eber, F. / Azucena, C. / Petershans, A. / Bittner, A. / Gliemann, H. / Jeske, H. / Wege, C. (2011): „ Inducible site-selective bottom-up assembly of virus-derived nanotube arrays on RNA-equipped wafers“. In: ACS Nano 5 (2011), 4512
Abstract
Tobacco mosaic virus (TMV) is a tube-shaped, exceptionally stable plant virus, which is among the biomolecule complexes offering most promising perspectives for nanotechnology applications. Every viral nanotube self-assembles from a single RNA strand and numerous identical coat protein (CP) subunits. Here we demonstrate that biotechnologically engineered RNA species containing the TMV origin of assembly can be selectively attached to solid surfaces via one end and govern the bottom-up growth of surface-linked TMV-like nanotubes in situ on demand. SiO2 wafers patterned by polymer blend lithography were modified in a chemically selective manner, which allowed positioning of in vitro produced RNA scaffolds into predefined patches on the 100–500 nm scale.
The RNA operated as guiding strands for the self-assembly of spatially ordered nanotube 3D arrays on the micrometer scale. This novel approach may promote technically applicable production routes toward a controlled integration of multivalent biotemplates into miniaturized devices to functionalize poorly accessible components prior to use. Furthermore, the results mark a milestone in the experimental verification of viral nucleoprotein complex self-assembly mechanisms.
The RNA operated as guiding strands for the self-assembly of spatially ordered nanotube 3D arrays on the micrometer scale. This novel approach may promote technically applicable production routes toward a controlled integration of multivalent biotemplates into miniaturized devices to functionalize poorly accessible components prior to use. Furthermore, the results mark a milestone in the experimental verification of viral nucleoprotein complex self-assembly mechanisms.
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