Rotary biomolecular motor-powered supramolecular colloidal motor.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 36812329.
- Also identified by DOI 10.1126/sciadv.abg3015 and PMC identifier 9946340.
- Licence recorded as CC BY-NC.
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Abstract
Cells orchestrate the motion and force of hundreds of protein motors to perform various mechanical tasks over multiple length scales. However, engineering active biomimetic materials from protein motors that consume energy to propel continuous motion of micrometer-sized assembling systems remains challenging. Here, we report rotary biomolecular motor-powered supramolecular (RBMS) colloidal motors that are hierarchically assembled from a purified chromatophore membrane containing F<sub>O</sub>F<sub>1</sub>-ATP synthase molecular motors, and an assembled polyelectrolyte microcapsule. The micro-sized RBMS motor with asymmetric distribution of F<sub>O</sub>F<sub>1</sub>-ATPases can autonomously move under light illumination and is collectively powered by hundreds of rotary biomolecular motors. The propulsive mechanism is that a transmembrane proton gradient generated by a photochemical reaction drives F<sub>O</sub>F<sub>1</sub>-ATPases to rotate for ATP biosynthesis, which creates a local chemical field for self-diffusiophoretic force. Such an active supramolecular architecture endowed with motility and biosynthesis offers a promising platform for intelligent colloidal motors resembling the propulsive units in swimming bacteria.
Medical subject headings
- Proton-Translocating ATPases
- Bacteria