Control of myosin motor activity by the reversible alteration of protein structure for application in a bionanodevice

The application of bionanomotors for the transport of nano-sized objects and molecular sorting is an area of growing interest. Bionanomotors are motor proteins that have capability to convert chemical form of energy into mechanical energy with a remarkable degree of efficiency. Myosin II is a motor protein that has crucial role in muscle contraction, cell division and transport of cellular traffic. The use of the myosin II bio-nanomotor for nanotechnological applications has been hampered by an inability to modulate enzyme activity in a controlled fashion. Herein we examine if inducing changes in myosin motor structure can be used to regulate motor activity. Our findings indicate that myosin motor activity can be effectively and repeatedly cycled by altering the oxidative status of the experimental environment and that this means of control is most likely due to the formation of disulfide bonds between two adjacent myosin essential light chains. This strategy, if refined further, may prove useful for harnessing the potential of the myosin bionanomotor for future ex vivo applications. © 2012 American Scientific Publishers. All rights reserved.