Directed formation of micro- and nanoscale patterns of functional light-harvesting LH2 complexes

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

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43 Citations (Scopus)


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.
Original languageUndefined
Pages (from-to)14625-14631
Number of pages7
JournalJournal of the American Chemical Society
Issue number47
Publication statusPublished - 2007


  • METIS-243370
  • IR-74644

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