Motility and structural polymorphism of polymer-actin complex gel.
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 ATP hydrolysis. 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.
Kwon
Hyuck Joon
HJ
Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
Shikinaka
Kazuhiro
K
Kakugo
Akira
A
Furukawa
Hidemitsu
H
Osada
Yoshihito
Y
Gong
Jian Ping
JP
D000199:Actins / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D005782:Gels; D006868:Hydrolysis; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D009038:Motion; D009218:Myosins / Q000737:chemistry; D036103:Nanotechnology; D049897:Pectinidae; D011073:Polyamines / Q000737:chemistry; D000071228:Polyelectrolytes; D011108:Polymers / Q000737:chemistry*; D055672:Static Electricity
D000199:Actins; D000255:Adenosine Triphosphate; D005782:Gels; D046911:Macromolecular Substances; D009218:Myosins; D011073:Polyamines; D000071228:Polyelectrolytes; D011108:Polymers