Int J Mol Sci
Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
Published: September 2008
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 F-actin, 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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http://dx.doi.org/10.3390/ijms9091685 | DOI Listing |
Int J Mol Sci
September 2008
Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
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 F-actin, 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.
View Article and Find Full Text PDFJ Nanosci Nanotechnol
March 2007
Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
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.
View Article and Find Full Text PDFBiomacromolecules
February 2006
Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan, and SORST, JST, Sapporo, 060-0810, Japan.
F-actins are semi-flexible polyelectrolytes and can be assembled into a large polymer-actin complex with polymorphism through electrostatic interaction with polycations. This study investigates the structural phase behavior and the growth of polymer-actin complexes in terms of its longitudinal and lateral sizes in various polycation and KCl concentrations for a constant actin concentration. Our results show that the longitudinal growth and lateral growth of polymer-actin complexes, initiated by a common nucleation process, are dominated by different factors in subsequent growth process.
View Article and Find Full Text PDFBiomacromolecules
August 2005
Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
The polarity of polymer-actin complexes obtained by mixing F-actin with synthetic polymers carrying positive charges such as poly(L-lysine), x,y-ionene bromide polymers, and poly(N-[3-(dimethylamino)propyl]acrylamide) (PDMAPAA-Q) have been investigated. Actin complexes formed with poly(L-lysine) and PDMAPAA-Q, which carry charges on their side chains, show a higher polarity than those formed with x,y-ionene bromide polymers, which have charges on their chain backbones. All these polymer-actin complex gels show motility on the surfaces coated with myosin by coupling to adenosine 5'-triphosphate hydrolysis.
View Article and Find Full Text PDFBioconjug Chem
July 2004
Graduate School of Science, Hokkaido University, Japan.
Polymer-actin complexes as large as 10-50 microm with filamentous, branched, stranded, and ring shapes are obtained when fluorescent phalloidin-labeled F-actin is mixed with some synthetic polymers carrying positive charges such as poly-L-lysine, x,y-ionene bromide polymers. All growth of these complexes occurs cooperatively at some certain critical polymer concentrations, regardless of the chemical structure of the polymer, while the morphology of the complexes is substantially influenced by the chemical structure of the polymer. Poly-Lys-actin complex grows preferentially along the filament axis even above the critical concentration.
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