4.5 Review

Reconstitution of FoF1-ATPase-based biomimetic systems

Journal

NATURE REVIEWS CHEMISTRY
Volume 3, Issue 6, Pages 361-374

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/s41570-019-0100-8

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Funding

  1. National Natural Science Foundation of China [21433010, 21872151, 21320102004]

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Nature makes use of molecular machines to perform intricate functions in every significant biological process and to power macroscopic motion in organisms. Biomolecular motor proteins perform crucial tasks such as cell division, intracellular transport and mechanical actuation in biological cells. The rotary motor FoF1-ATPase is one of the most extensively studied biomolecular machines as a result of its vital physiological function. Research on the function of FoF1-ATPase can help to better understand the underlying biological processes and may also result in the development of biological molecular motor-based devices or even inspire the creative design and construction of artificial molecular machines. Recent advances in nanoscience and biotechnology have enabled engineering experiments with FoF1-ATPase that have achieved notable success. In this Review, we first outline the reconstitution of FoF1-ATPase into simple liposomes and polymersomes and then focus on recent progress in the reconstitution of FoF1-ATPase on layer-by-layer-assembled systems. The elaborate structural designs utilized in layer-by-layer-assembled systems to better mimic natural cell structures are introduced. The rational integration of functional components to achieve stimuli-responsive ATP syntheses from FoF1-ATPase-based biomimetic systems is highlighted. Finally, we address some remaining key challenges and speculate on future directions for the field.

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