Self-assembly of F0F1-ATPase motors and ghost.
F0F1-ATPase motors have unique mechanical properties, making them attractive building blocks in the field of nanotechnology. However, their organization into well-defined structures with practical functions remains a critical challenge. Here, we describe a self-assembling complex formed by F0F1-ATPase and a ghost which is ordered. Formation of the complex includes two steps: the molecular motors first self-assemble into filaments and then attach to the ghost. The ghost and attached filaments then aggregate into large self-assembled complexes. On illumination, these complexes disassemble because of the rotation force of the molecular motors. The complexes are macroscopic, having a diameter greater than 1 mm. Such complexes of a flexible biomaterial (ghost) self-assembled with a dynamic biomaterial (F0F1-ATPase molecular motor) have several advantages, including flexibility, stability, and ability to be controlled by light, and could be used as controllable rotational molecular machines.
Tao
Ning
N
The National Laboratory of Biomacromolecules, Institute of Biophysics, Graduate School, Chinese Academy of Sciences, Beijing 100101, China.
Cheng
Jie
J
Wei
Ling
L
Yue
Jiachang
J
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry*; D004910:Erythrocyte Membrane / Q000737:chemistry*; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D012247:Rhodospirillum rubrum / Q000201:enzymology*; D013552:Swine
D001426:Bacterial Proteins; D006180:Proton-Translocating ATPases