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Int. J. Mol. Sci. 2008, 9(9), 1685-1703;

Integration of Motor Proteins – Towards an ATP Fueled Soft Actuator

Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan
Author to whom correspondence should be addressed.
Received: 18 June 2008 / Revised: 8 August 2008 / Accepted: 27 August 2008 / Published: 4 September 2008
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We present a soft bio-machine constructed from biological motors (actin/myosin). We have found that chemically cross-linked polymer-actin complex gel filaments can move on myosin coated surfaces with a velocity as high as that of native Factin, by coupling to ATP hydrolysis. Additionally, it is shown that the velocity of polymer-actin complex gel depends on the species of polycations binding to the F-actins. Since the design of functional actuators of well-defined size and morphology is important, the structural behavior of polymer-actin complexes has been investigated. Our results show that the morphology and growth size of polymer-actin complex can be controlled by changes in the electrostatic interactions between F-actins and polycations. Our results indicate that bio actuators with desired shapes can be created by using a polymer-actin complex. View Full-Text
Keywords: Biological motors; self-assembly; hierarchical structure; soft-bio-machine Biological motors; self-assembly; hierarchical structure; soft-bio-machine
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Kakugo, A.; Shikinaka, K.; Gong, J.P. Integration of Motor Proteins – Towards an ATP Fueled Soft Actuator. Int. J. Mol. Sci. 2008, 9, 1685-1703.

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