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In situ enzymatic control of colloidal phoresis and catalysis through hydrolysis of ATP

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  • Ekta Shandilya

    (Indian Institute of Science Education and Research (IISER))

  • Bhargav Rallabandi

    (University of California)

  • Subhabrata Maiti

    (Indian Institute of Science Education and Research (IISER))

Abstract

The ability to sense chemical gradients and respond with directional motility and chemical activity is a defining feature of complex living systems. There is a strong interest among scientists to design synthetic systems that emulate these properties. Here, we realize and control such behaviors in a synthetic system by tailoring multivalent interactions of adenosine nucleotides with catalytic microbeads. We first show that multivalent interactions of the bead with gradients of adenosine mono-, di- and trinucleotides (AM/D/TP) control both the phoretic motion and a proton-transfer catalytic reaction, and find that both effects are diminished greatly with increasing valence of phosphates. We exploit this behavior by using enzymatic hydrolysis of ATP to AMP, which downregulates multivalent interactivity in situ. This produces a sudden increase in transport of the catalytic microbeads (a phoretic jump), which is accompanied by increased catalytic activity. Finally, we show how this enzymatic activity can be systematically tuned, leading to simultaneous in situ spatial and temporal control of the location of the microbeads, as well as the products of the reaction that they catalyze. These findings open up new avenues for utilizing multivalent interaction-mediated programming of complex chemo-mechanical behaviors into active systems.

Suggested Citation

  • Ekta Shandilya & Bhargav Rallabandi & Subhabrata Maiti, 2024. "In situ enzymatic control of colloidal phoresis and catalysis through hydrolysis of ATP," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-47912-2
    DOI: 10.1038/s41467-024-47912-2
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    References listed on IDEAS

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    1. Aitao Li & Binju Wang & Adriana Ilie & Kshatresh D. Dubey & Gert Bange & Ivan V. Korendovych & Sason Shaik & Manfred T. Reetz, 2017. "A redox-mediated Kemp eliminase," Nature Communications, Nature, vol. 8(1), pages 1-8, April.
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    Cited by:

    1. Suin Shim & Bernardo Gouveia & Beatrice Ramm & Venecia A. Valdez & Sabine Petry & Howard A. Stone, 2024. "Motorless transport of microtubules along tubulin, RanGTP, and salt gradients," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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