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

Research output: Contribution to journalArticleAcademicpeer-review

41 Citations (Scopus)

Abstract

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
Volume129
Issue number47
DOIs
Publication statusPublished - 2007

Keywords

  • METIS-243370
  • IR-74644

Cite this

Reynolds, N. P., Janusz, S., Escalante Marun, M., Escalante-Marun, M., Timney, J., Ducker, R. E., ... Hunter, C. N. (2007). Directed formation of micro- and nanoscale patterns of functional light-harvesting LH2 complexes. Journal of the American Chemical Society, 129(47), 14625-14631. https://doi.org/10.1021/ja073658m
Reynolds, Nicholas P. ; Janusz, Stefan ; Escalante Marun, M. ; Escalante-Marun, Maryana ; Timney, John ; Ducker, Robert E. ; Olsen, John D. ; Otto, Cornelis ; Subramaniam, Vinod ; Leggett, Graham J. ; Hunter, C. Neil. / Directed formation of micro- and nanoscale patterns of functional light-harvesting LH2 complexes. In: Journal of the American Chemical Society. 2007 ; Vol. 129, No. 47. pp. 14625-14631.
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abstract = "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.",
keywords = "METIS-243370, IR-74644",
author = "Reynolds, {Nicholas P.} and Stefan Janusz and {Escalante Marun}, M. and Maryana Escalante-Marun and John Timney and Ducker, {Robert E.} and Olsen, {John D.} and Cornelis Otto and Vinod Subramaniam and Leggett, {Graham J.} and Hunter, {C. Neil}",
year = "2007",
doi = "10.1021/ja073658m",
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volume = "129",
pages = "14625--14631",
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Reynolds, NP, Janusz, S, Escalante Marun, M, Escalante-Marun, M, Timney, J, Ducker, RE, Olsen, JD, Otto, C, Subramaniam, V, Leggett, GJ & Hunter, CN 2007, 'Directed formation of micro- and nanoscale patterns of functional light-harvesting LH2 complexes', Journal of the American Chemical Society, vol. 129, no. 47, pp. 14625-14631. https://doi.org/10.1021/ja073658m

Directed formation of micro- and nanoscale patterns of functional light-harvesting LH2 complexes. / Reynolds, Nicholas P.; Janusz, Stefan; Escalante Marun, M.; Escalante-Marun, Maryana; Timney, John; Ducker, Robert E.; Olsen, John D.; Otto, Cornelis; Subramaniam, Vinod; Leggett, Graham J.; Hunter, C. Neil.

In: Journal of the American Chemical Society, Vol. 129, No. 47, 2007, p. 14625-14631.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Directed formation of micro- and nanoscale patterns of functional light-harvesting LH2 complexes

AU - Reynolds, Nicholas P.

AU - Janusz, Stefan

AU - Escalante Marun, M.

AU - Escalante-Marun, Maryana

AU - Timney, John

AU - Ducker, Robert E.

AU - Olsen, John D.

AU - Otto, Cornelis

AU - Subramaniam, Vinod

AU - Leggett, Graham J.

AU - Hunter, C. Neil

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

KW - METIS-243370

KW - IR-74644

U2 - 10.1021/ja073658m

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JF - Journal of the American Chemical Society

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Reynolds NP, Janusz S, Escalante Marun M, Escalante-Marun M, Timney J, Ducker RE et al. Directed formation of micro- and nanoscale patterns of functional light-harvesting LH2 complexes. Journal of the American Chemical Society. 2007;129(47):14625-14631. https://doi.org/10.1021/ja073658m