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

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

    Research output: Contribution to JournalArticleAcademicpeer-review


    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 languageEnglish
    Pages (from-to)14625-31
    Number of pages7
    JournalJournal of the American Chemical Society
    Issue number47
    Publication statusPublished - 28 Nov 2007


    • Binding Sites
    • Light-Harvesting Protein Complexes
    • Microscopy, Atomic Force
    • Nanostructures
    • Photochemistry
    • Rhodobacter sphaeroides
    • Substrate Specificity
    • Surface Plasmon Resonance
    • Journal Article
    • Research Support, Non-U.S. Gov't


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