Thermally responsive supramolecular nanomeshes for on/off switching of the rotary motion of F1-ATPase at the single-molecule level.
The artificial regulation of protein functions is essential for the realization of protein-based soft devices, because of their unique functions conducted within a nano-sized molecular space. We report that self-assembled nanomeshes comprising heat-responsive supramolecular hydrogel fibers can control the rotary motion of an enzyme-based biomotor (F(1)-ATPase) in an on/off manner at the single-molecule level. Direct observation of the interaction of the supramolecular fibers with a microbead unit tethered to the F(1)-ATPase and the clear threshold in the size of the bead required to stop ATPase rotation indicates that the bead was physically blocked so as to stop the rotary motion of ATPase. The temperature-induced formation and collapse of the supramolecular nanomesh can produce or destroy, respectively, the physical obstacle for ATPase so as to control the ATPase motion in an off/on manner. Furthermore, this switching of the F(1)-ATPase motion could be spatially restricted by using a microheating device. The integration of biomolecules and hard materials, interfaced with intelligent soft materials such as supramolecular hydrogels, is promising for the development of novel semi-synthetic nano-biodevices.
PRESTO (Synthesis and Control, JST), Kyoto University, Katsura, Nishikyo-Ku, Kyoto, 615-8510, Japan.
Satoshi
S
Yamaguchi
Shinji
S
Matsumoto
Koji
K
Ishizuka
Yuko
Y
Iko
Kazuhito V
KV
Tabata
Hideyuki F
HF
Arata
Hiroyuki
H
Fujita
Hiroyuki
H
Noji
Itaru
I
Hamachi
D036103:Nanotechnology; D006180:Proton-Translocating ATPases / Q000737:chemistry*
D006180:Proton-Translocating ATPases