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Integration of Motor Proteins – Towards an ATP Fueled Soft Actuator
AbstractWe 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.
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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.View more citation formats
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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