Choi, D. S., Byun, K.-E., & Hong, S.
Department of Physics and Astronomy Seoul National University Seoul, 151–747, Department of Biophysics and Chemical Biology Seoul National University Seoul, Department of Nano Science and Engineering Seoul National University Seoul, 151–747, Korea, Department of Nano Science and Engineering Seoul National University Seoul, 151–747, Korea, Department of Physics and Astronomy Seoul National University Seoul, 151–747, Korea.
General Fluorescence Microscopy
Motor proteins are highly efficient engines that convert the chemical energy of adenosine triphosphate (ATP) into mechanical energy. [ 1 ] Two representative motor proteins, kinesin and myosin , interact with different cytoskeletal elements, microtubules (MTs) and actin fi laments (AFs), respectively. Thanks to the development of in-vitro assays for those proteins, motor proteins have been extensively studied and considered as a basic building block for nanotransportation devices. [ 2–5 ] For example, either MTs on kinesin or AFs on myosin have been utilized as a nanoshuttle that can carry various nanostructures such as viruses, [ 6,7 ] DNAs, [ 8–10 ] quantum dots, [ 11–13 ] and nanoparticles. [ 14 ] Transportation devices based on each motor protein have different advantages. MTs on kinesin tend to move straight, due to its rigid structure, and AFs on myosin have rather curved trajectories with fast gliding speeds. Therefore, kinesin-based devices are suitable for stable transportation over a long distance, while myosin-based ones can be useful in picking up cargo in highly miniaturized, curved tracks. [ 2 , 15,16 ] Although the necessity of an integrated device including both motor proteins has been addressed before, [ 2 ] kinesin and myosin motor proteins were believed to be incompatible, and previous nanotransporta- tion systems based on MTs or AFs have been investigated exclusively either on kinesin or myosin. Such incompatibility between the two motor protein systems lowered the flexibility of device design and eventually limited the possible applications of protein motor-based nanotransport systems. Herein, we develop microtubule–actin fi lament (MT–AF) hybrid nanostructures which can work as a nanotransportation system on both kinesin and myosin coated surfaces. In this work, the MT–AF hybrid nanostructures are constructed by conjugating MTs and AFs with biotin–streptavidin bonds. The motility of the MT–AF hybrid nanostructures is success- fully demonstrated on both kinesin and myosin-coated surfaces. Interestingly, the analysis of their trajectories reveals that the MT–AF hybrid nanostructures exhibited AF- or MT- like motions on myosin or kinesin, respectively. This hybrid nanostructure can be a simple but versatile platform for developing a nanotransportation system that can take advantage of these two different motor proteins.
… “and CoolLED (Custom Inter- connect Ltd.) was used as the light source to illuminate differently labelled filaments.”…
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pE-100: A range of compact, simple-to-use, single wavelength illumination systems for screening fluorescence.
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