Powering an inorganic nanodevice with a biomolecular motor.
Biomolecular motors such as F1-adenosine triphosphate synthase (F1-ATPase) and myosin are similar in size, and they generate forces compatible with currently producible nanoengineered structures. We have engineered individual biomolecular motors and nanoscale inorganic systems, and we describe their integration in a hybrid nanomechanical device powered by a biomolecular motor. The device consisted of three components: an engineered substrate, an F1-ATPase biomolecular motor, and fabricated nanopropellers. Rotation of the nanopropeller was initiated with 2 mM adenosine triphosphate and inhibited by sodium azide.
Soong
R K
RK
Nanobiotechnology Center, Department of Agricultural and Biological Engineering, School of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853, USA.
Bachand
G D
GD
Neves
H P
HP
Olkhovets
A G
AG
Craighead
H G
HG
Montemagno
C D
CD
D000255:Adenosine Triphosphate / Q000378:metabolism; D001709:Biotechnology / Q000295:instrumentation / Q000379:methods; D019921:Biotinylation; D004791:Enzyme Inhibitors; D008904:Miniaturization; D020409:Molecular Motor Proteins; D009532:Nickel / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000378:metabolism; D011994:Recombinant Proteins; D012399:Rotation; D019810:Sodium Azide / Q000494:pharmacology
D004791:Enzyme Inhibitors; D020409:Molecular Motor Proteins; D011994:Recombinant Proteins; D009532:Nickel; D000255:Adenosine Triphosphate; D019810:Sodium Azide; D006180:Proton-Translocating ATPases