Directed Formation of Micro- and Nanoscale Patterns of Functional Light-Harvesting LH2 Complexes Academic Article uri icon


  • The precision placement of the desired protein components on a suitable substrate is an essential prelude to any hybrid "biochip" device, but a second and equally important condition must also be met: the retention of full biological activity. Here we demonstrate the selective binding of an optically active membrane protein, the light-harvesting LH2 complex from Rhodobacter sphaeroides, to patterned self-assembled monolayers at the micron scale and the fabrication of nanometer-scale patterns of these molecules using near-field photolithographic methods. In contrast to plasma proteins, which are reversibly adsorbed on many surfaces, the LH2 complex is readily patterned simply by spatial control of surface polarity. Near-field photolithography has yielded rows of light-harvesting complexes only 98 nm wide. Retention of the native optical properties of patterned LH2 molecules was demonstrated using in situ fluorescence emission spectroscopy.


  • Reynolds, Nicholas P
  • Janusz, Stefan
  • Escalante-Marun, Maryana
  • Timney, John
  • Ducker, Robert E
  • Olsen, John D
  • Otto, Cees
  • Subramaniam, Vinod
  • Leggett, Graham J
  • Hunter, C Neil

publication date

  • November 2007