Directed formation of micro- and nanoscale patterns of functional light-harvesting LH2 complexes.
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
NP
Department of Chemistry, University of Sheffield, UK.
Janusz
Stefan
S
Escalante-Marun
Maryana
M
Timney
John
J
Ducker
Robert E
RE
Olsen
John D
JD
Otto
Cees
C
Subramaniam
Vinod
V
Leggett
Graham J
GJ
Hunter
C Neil
CN
D001665:Binding Sites; D045342:Light-Harvesting Protein Complexes / Q000378:metabolism*; D018625:Microscopy, Atomic Force; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure; D010777:Photochemistry; D012242:Rhodobacter sphaeroides / Q000201:enzymology; D013379:Substrate Specificity; D020349:Surface Plasmon Resonance
D045342:Light-Harvesting Protein Complexes