Powering an inorganic nanodevice with a biomolecular motor

R. K. Soong; G. D. Bachand; H. P. Neves; A. G. Olkhovets; H. G. Craighead; C. D. Montemagno

doi:10.1126/science.290.5496.1555

Powering an inorganic nanodevice with a biomolecular motor

R. K. Soong, G. D. Bachand, H. P. Neves, A. G. Olkhovets, H. G. Craighead, C. D. Montemagno

Research output: Contribution to journal › Article › peer-review

566 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	1555-1558
Number of pages	4
Journal	Science
Volume	290
Issue number	5496
DOIs	https://doi.org/10.1126/science.290.5496.1555
State	Published - Nov 24 2000

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abstract = "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.",

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AU - Bachand, G. D.

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AU - Craighead, H. G.

AU - Montemagno, C. D.

PY - 2000/11/24

Y1 - 2000/11/24

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AB - 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.

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Powering an inorganic nanodevice with a biomolecular motor

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