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Motility and Structural Polymorphism of Polymer–Actin Complex Gel

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Abstract:

We report a soft gel machine reconstructed from muscle proteins. We have found that chemically cross-linked polymer–actin complex gel can move on myosin coated surface with a velocity as high as that of native F-actin, by coupling to ATPhydrolysis. Additionally, it is shown that the velocity and motional pattern of polymer–actin complex gel depends on the morphology of polymer-complex gels. Since the designing of functional actuator into well-defined size and morphology is important, the structural behavior of polymer–actin complexes has been investigated. This result shows that the morphology and growth size of polymer–actin complex can be controlled by change of electrostatic interaction between F-actins and polycations. Our results indicate that bio actuator with desired shape can be created by using polymer–actin complex.

Keywords: ACTIN; MYOSIN; POLYCATION; POLYMER-ACTIN COMPLEX; POLYMER-ACTIN COMPLEX GEL

Document Type: Research Article

DOI: http://dx.doi.org/10.1166/jnn.2007.510

Publication date: March 1, 2007

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  • Journal for Nanoscience and Nanotechnology (JNN) is an international and multidisciplinary peer-reviewed journal with a wide-ranging coverage, consolidating research activities in all areas of nanoscience and nanotechnology into a single and unique reference source. JNN is the first cross-disciplinary journal to publish original full research articles, rapid communications of important new scientific and technological findings, timely state-of-the-art reviews with author's photo and short biography, and current research news encompassing the fundamental and applied research in all disciplines of science, engineering and medicine.
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