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Sustained enzymatic activity and flow in crowded protein droplets

Author

Listed:
  • Andrea Testa

    (ETH Zürich)

  • Mirco Dindo

    (Okinawa Institute of Science and Technology Graduate University)

  • Aleksander A. Rebane

    (ETH Zürich)

  • Babak Nasouri

    (Max Planck Institute for Dynamics and Self-Organization (MPIDS))

  • Robert W. Style

    (ETH Zürich)

  • Ramin Golestanian

    (Max Planck Institute for Dynamics and Self-Organization (MPIDS)
    University of Oxford)

  • Eric R. Dufresne

    (ETH Zürich)

  • Paola Laurino

    (Okinawa Institute of Science and Technology Graduate University)

Abstract

Living cells harvest energy from their environments to drive the chemical processes that enable life. We introduce a minimal system that operates at similar protein concentrations, metabolic densities, and length scales as living cells. This approach takes advantage of the tendency of phase-separated protein droplets to strongly partition enzymes, while presenting minimal barriers to transport of small molecules across their interface. By dispersing these microreactors in a reservoir of substrate-loaded buffer, we achieve steady states at metabolic densities that match those of the hungriest microorganisms. We further demonstrate the formation of steady pH gradients, capable of driving microscopic flows. Our approach enables the investigation of the function of diverse enzymes in environments that mimic cytoplasm, and provides a flexible platform for studying the collective behavior of matter driven far from equilibrium.

Suggested Citation

  • Andrea Testa & Mirco Dindo & Aleksander A. Rebane & Babak Nasouri & Robert W. Style & Ramin Golestanian & Eric R. Dufresne & Paola Laurino, 2021. "Sustained enzymatic activity and flow in crowded protein droplets," Nature Communications, Nature, vol. 12(1), pages 1-8, December.
  • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26532-0
    DOI: 10.1038/s41467-021-26532-0
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    References listed on IDEAS

    as
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