Stretching and Transporting DNA Molecules Using Motor Proteins

Diez, Stefan; Reuther, Cordula; Dinu, Cerasela Zoica; Seidel, Ralf; Mertig, Michael; Pompe, W.; Howard, Jonathon

doi:10.1021/nl034504h

Cited by 156 publications

(122 citation statements)

References 45 publications

(69 reference statements)

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“…[85,86] Similarly, the motility of microtubules powered by kinesin has also been demonstrated on surfaces, such as glass, [75,[87][88][89][90][91] PTFE, [35] deepUV resist (SAL601), [37] silicon, [87] PMMA, [88] poly(dimethylsiloxane) (PDMS), [88] ethylene-vinyl alcohol copolymer (EVOH), [88] thermoresponsive poly(Nisopropylacrylamide) (PNIPAM) grafted onto polyglycidyl methacrylate (PGMA), [92] and reconstituted microtubules. [93] Some features worth noting are that different surfaces induce differential adsorption of proteins (i.e., BSA and motors) and small variations in experimental conditions can lead to entirely different motilities.…”

Section: Surface Effectsmentioning

confidence: 99%

“…These include devices that operate in fluid environments that have very few, nondeactivating, chemical species (e.g., oligonucleotides [89] ), and which operate under controlled conditions (e.g., temperature and pH). Alternatively, one can consider applications where it is precisely the deactivation of the motility by the fluid environment that constitutes the function of the device (e.g., detection by heavy metal ions [107] ).…”

Section: Toxicitymentioning

confidence: 99%

“…[89,107] The inhibition of microtubule-based kinesin motility using local anaesthetics has been demonstrated [136] and a pausing effect can be provided by electric fields that are capable of docking microtubules. [137] Microtubules have been shown to be repelled by thermoresponsive PNIPAM when the surface was cooled and re-permitted to glide when heated.…”

Section: On-off Control Of the Operation Of Proteinmentioning

confidence: 99%

“…on the motile elements. This principle has been demonstrated for (i) microtubules decorated with streptavidin that detect and stretch biotin-terminated λ-phase DNA molecules, [89] (ii) detection of antigens through the cessation of the motility of actin filaments decorated with antibodies, [144] which include more selective streptavidin-antibody multilayer sandwiches biotinylated to microtubules. [145] Figure 7 presents two possibilities for distributed nanobiosensing devices.…”

Section: Sensing Devicesmentioning

confidence: 99%

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Protein Linear Molecular Motor‐Powered Nanodevices

Bakewell

Nicolau

2007

ChemInform

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Myosin-actin and kinesin-microtubule linear protein motor systems and their application in hybrid nanodevices are reviewed. Research during the past several decades has provided a wealth of understanding about the fundamentals of protein motors that continues to be pursued. It has also laid the foundations for a new branch of investigation that considers the application of these motors as key functional elements in laboratory-on-a-chip and other micro/nanodevices. Current models of myosin and kinesin motors are introduced and the effects of motility assay parameters, including temperature, toxicity, and in particular, surface effects on motor protein operation, are discussed. These parameters set the boundaries for gliding and bead motility assays. The review describes recent developments in assay motility confinement and unidirectional control, using micro-and nano-fabricated structures, surface patterning, microfluidic flow, electromagnetic fields, and self-assembled actin filament/microtubule tracks. Current protein motor assays are primitive devices, and the developments in governing control can lead to promising applications such as sensing, nano-mechanical drivers, and biocomputation.

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Section: Surface Effectsmentioning

confidence: 99%

Section: Toxicitymentioning

confidence: 99%

Section: On-off Control Of the Operation Of Proteinmentioning

confidence: 99%

Section: Sensing Devicesmentioning

confidence: 99%

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Protein Linear Molecular Motor‐Powered Nanodevices

Bakewell

Nicolau

2007

ChemInform

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“…In the last decade, remarkable progress has been made in the applications of motor proteins in microscale and nanoscale engineering, which has enabled the control of motor protein movements and the transport of artificial objects by motor protein (2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14). These microtransportation systems are expected to be a shuttle for micrototal analysis systems and other simple tools (15)(16)(17).…”

mentioning

confidence: 99%

Self-organized optical device driven by motor proteins

Aoyama

Shimoike

Hiratsuka

2013

Proc. Natl. Acad. Sci. U.S.A.

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Protein molecules produce diverse functions according to their combination and arrangement as is evident in a living cell. Therefore, they have a great potential for application in future devices. However, it is currently very difficult to construct systems in which a large number of different protein molecules work cooperatively. As an approach to this challenge, we arranged protein molecules in artificial microstructures and assembled an optical device inspired by a molecular system of a fish melanophore. We prepared arrays of cell-like microchambers, each of which contained a scaffold of microtubule seeds at the center. By polymerizing tubulin from the fixed microtubule seeds, we obtained radially arranged microtubules in the chambers. We subsequently prepared pigment granules associated with dynein motors and attached them to the radial microtubule arrays, which made a melanophore-like system. When ATP was added to the system, the color patterns of the chamber successfully changed, due to active transportation of pigments. Furthermore, as an application of the system, image formation on the array of the optical units was performed. This study demonstrates that a properly designed microstructure facilitates arrangement and selforganization of molecules and enables assembly of functional molecular systems.bioengineering | microdevice | molecular robotics W ithin a cell, motor proteins work as mechanical components that efficiently convert chemical energy to mechanical energy. Major motor proteins, such as myosin, kinesin, and dynein, travel unidirectionally along specific filamentous protein polymers, actin filaments, or microtubules, using the chemical energy derived from ATP. Although the action of motor proteins itself is rather simple, they are involved in numerous functions in living cells such as cell division, muscle contractions, ciliary beating, and melanophore color changes (1). These diverse and elaborate functions are realized through highly ordered molecular systems that consist of not only the motor proteins but also various types of protein molecules. For example, myosin and actin form alternatively arranged bundles with tens of other proteins to construct aligned sarcomeres, the basic units of the muscle, which produce efficient contractions under strict Ca 2+ regulation (1). Likewise, in the cilium or flagellum, dynein molecules are integrated into the "9 + 2" arrangement of microtubules and generate oscillatory bending (1). Thus, diversity of in vivo functions of motor proteins is achieved by the variety of manners in which motor proteins are organized into specific higher order systems.In the last decade, remarkable progress has been made in the applications of motor proteins in microscale and nanoscale engineering, which has enabled the control of motor protein movements and the transport of artificial objects by motor protein (2-14). These microtransportation systems are expected to be a shuttle for micrototal analysis systems and other simple tools (15)(16)(17). To fully use the potential...

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