Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 129, Issue 47, Pages 14625-14631Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja073658m
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- Engineering and Physical Sciences Research Council [EP/C523857/1] Funding Source: researchfish
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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.
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