Institut für Funktionelle Grenzflächen (IFG)

New Approaches for Bottom-Up Assembly of Tobacco Mosaic Virus-Derived Nucleoprotein Tubes on Defined Patterns on Silica- and Polymer-Based Substrates

  • Autor:

    Azucena, C. / Eber, F. / Trouillet, V. / Hirtz, M. / Heissler, S. / Franzreb, M. / Fuchs, H. / Wege, C. / Gliemann, H. (2012)

  • Quelle:

    Langmuir 28 (2012), 42, 14867–14877

  • Datum: 2012
  • Azucena, C. / Eber, F. / Trouillet, V. / Hirtz, M. / Heissler, S. / Franzreb, M. / Fuchs, H. / Wege, C. / Gliemann, H. (2012): „New Approaches for Bottom-Up Assembly of Tobacco Mosaic Virus-Derived Nucleoprotein Tubes on Defined Patterns on Silica- and Polymer-Based Substrates“. In: Langmuir 28 (2012), 42, 14867–14877

Abstract

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The capability of some natural molecular building blocks to self-organize into defined supramolecular architectures is a versatile tool for nanotechnological applications. Their site-selective integration into a technical context, however, still poses a major challenge.

RNA-directed self-assembly of tobacco mosaic virus-derived coat protein on immobilized RNA scaffolds presents a possibility to grow nucleoprotein nanotubes in place. Two new methods for their site-selective, bottom-up assembly are introduced.

For this purpose, isothiocyanate alkoxysilane was used to activate oxidic surfaces for the covalent immobilization of DNA oligomers, which served as linkers for assembly-directing RNA. Patterned silanization of surfaces was achieved on oxidic surfaces via dip-pen nanolithography and on polymer surfaces (poly(dimethylsiloxane)) via selective oxidization by UV-light irradiation in air.

Atomic force microscopy and X-ray photoelectron spectroscopy were used to characterize the surfaces. It is shown for the first time that the combination of the mentioned structuring methods and the isothiocyanate-based chemistry is appropriate for the site-selective immobilization of nucleic acids and, thus, for the formation of viral nanoparticles by bottom-up self-assembly after adding the corresponding coat proteins.