| 초록 |
Motor proteins, such as actin-myosin system and microtubule-kinesin system, have been proposed as the building blocks of ATP-fueled bio-machines. The greatest difficulties are how to exploit their sophisticated functions as high as that in cells and tissues. We report that large linear-shaped actin bundles, which consist of several tens of filament actin (F-actin), can be obtained through an electrostatic interaction with synthetic polymers carrying positive charges. In the presence of adenosine tri-phosphate (ATP), these bundles show motility on the surface coated with myosin that is a motor protein. We also report that large ring-shaped microtubule (MTs) bundles with a diameter of 1~12m can be obtained by integrating and simultaneously cross-linking MTs prepared in the presence of guanosine-5’-triphosphate (GTP) through streptavidin-biotin interaction during the sliding motion on the surface coated with kinesin that is a microtubule based motor protein. Interestingly, these ring shaped MT assembles show a preferential rotation. Under optimized conditions, the ratio of the rings rotating in the anti-clockwise direction to those rotating in the clockwise direction was reached 14/1. These results indicate that actins or MTs can be integrated into large assemblies without sacrificing their bioactivities through a static or dynamic self-assembly process in vitro. Here, we present an ATP fueled soft-actuator based on biomolecular motors with well ordered structure. |
