Int. J. Mol. Sci. 2008, 9(9), 1685-1703; doi:10.3390/ijms9091685

Integration of Motor Proteins – Towards an ATP Fueled Soft Actuator

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Received: 18 June 2008; in revised form: 8 August 2008 / Accepted: 27 August 2008 / Published: 4 September 2008
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract: 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.
Keywords: Biological motors; self-assembly; hierarchical structure; soft-bio-machine
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MDPI and ACS Style

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.

AMA Style

Kakugo A, Shikinaka K, Gong JP. Integration of Motor Proteins – Towards an ATP Fueled Soft Actuator. International Journal of Molecular Sciences. 2008; 9(9):1685-1703.

Chicago/Turabian Style

Kakugo, Akira; Shikinaka, Kazuhiro; Gong, Jian P. 2008. "Integration of Motor Proteins – Towards an ATP Fueled Soft Actuator." Int. J. Mol. Sci. 9, no. 9: 1685-1703.

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