Author
Listed:
- Alexander Ohmann
(University of Cambridge)
- Chen-Yu Li
(University of Illinois at Urbana-Champaign)
- Christopher Maffeo
(University of Illinois at Urbana-Champaign)
- Kareem Al Nahas
(University of Cambridge)
- Kevin N. Baumann
(University of Cambridge)
- Kerstin Göpfrich
(University of Cambridge)
- Jejoong Yoo
(University of Illinois at Urbana-Champaign)
- Ulrich F. Keyser
(University of Cambridge)
- Aleksei Aksimentiev
(University of Illinois at Urbana-Champaign
University of Illinois at Urbana-Champaign
University of Illinois at Urbana-Champaign)
Abstract
Mimicking enzyme function and increasing performance of naturally evolved proteins is one of the most challenging and intriguing aims of nanoscience. Here, we employ DNA nanotechnology to design a synthetic enzyme that substantially outperforms its biological archetypes. Consisting of only eight strands, our DNA nanostructure spontaneously inserts into biological membranes by forming a toroidal pore that connects the membrane’s inner and outer leaflets. The membrane insertion catalyzes spontaneous transport of lipid molecules between the bilayer leaflets, rapidly equilibrating the lipid composition. Through a combination of microscopic simulations and fluorescence microscopy we find the lipid transport rate catalyzed by the DNA nanostructure exceeds 107 molecules per second, which is three orders of magnitude higher than the rate of lipid transport catalyzed by biological enzymes. Furthermore, we show that our DNA-based enzyme can control the composition of human cell membranes, which opens new avenues for applications of membrane-interacting DNA systems in medicine.
Suggested Citation
Alexander Ohmann & Chen-Yu Li & Christopher Maffeo & Kareem Al Nahas & Kevin N. Baumann & Kerstin Göpfrich & Jejoong Yoo & Ulrich F. Keyser & Aleksei Aksimentiev, 2018.
"A synthetic enzyme built from DNA flips 107 lipids per second in biological membranes,"
Nature Communications, Nature, vol. 9(1), pages 1-9, December.
Handle:
RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04821-5
DOI: 10.1038/s41467-018-04821-5
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