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.J. / Trouillet, V. / Hirtz, M. / Heissler, S. / Franzreb, M. / Fuchs, H. / Wege, Ch. / Gliemann, H. (2012)

  • Quelle:

    Langmuir, 28(2012) S.14867-14877

  • Datum: 2012
  • Azucena, C. / Eber, F.J. / Trouillet, V. / Hirtz, M. / Heissler, S. / Franzreb, M. / Fuchs, H. / Wege, Ch. / 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) S.14867-14877 (2012)

Abstract

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 (1) on oxidic surfaces via dip-pen nanolithography and (2) 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 (1) for the site-selective immobilization of nucleic acids and, thus, (2) for the formation of viral nanoparticles by bottom-up self-assembly after adding the corresponding coat proteins.



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