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.
The National Laboratory of Biomacromolecules, Institute of Biophysics, Graduate School, Chinese Academy of Sciences, Beijing 100101, China.
Ning
N
Tao
Jie
J
Cheng
Ling
L
Wei
Jiachang
J
Yue
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