Protein motors are chemo-mechanical ATPases that can naturally generate force and move cargo or as individual molecules along tracks of protein polymers (actin filaments or microtubules), using chemical energy from adenosinetriphosphate (ATP) hydrolysis. In order to harness these protein motors to power nanometer-scale devices, we have investigated effective and non-destructive methods for immobilizing them and/or their protein filament tracks on surfaces and to steer the output of these motors, i.e. force and movement, into defined directions. We succeeded in aligning protein motors (myosin and its proteolytic fragments) on microscopic tracks composed of polytetrafluoroethylene (PTFE) deposited on the surfaces or polymethylmethacrylate (PMMA) prepared lithographically. Control of protein-motor driven movement of protein filaments was successfully made by using micrometer-scale grooves or walls lithographically fabricated on glass surfaces, and thus unidirectional movement of the filaments was accomplished by adding simple patterns onto the grooves or walls.
