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April 12, 2026Nature Communications1 citationsOpen Access

Gallium in liquid state shows nuclease-mimicking activity

LLLi LiuJZJiewei ZhengXLXi Lu

Key Points

  • The aim is to investigate gallium's ability to mimic nuclease activity using minimal components.
  • Demonstrated gallium's performance in liquid state for nuclease-like activity.
  • Analyzed the mechanism involving hydroxyl radical-assisted phosphodiester hydrolysis.
  • Evaluated the tunability of gallium's activity through synthesis parameters and external stimuli.
  • Gallium uniquely integrates an oxide layer for substrate adsorption.
  • The metallic core allows for cleavage activity without ligands or cofactors.
  • Introduced a minimalistic platform for artificial nuclease with programmable control.

Abstract

Abstract Replicating biological systems using non-living materials, from the foundational molecular level to complex tissue structures, is central to abiotic mimicry. Enzymes play a vital role in these systems; however, replicating their enzymatic power with minimal components remains a key challenge. Here we show that gallium in the liquid state exhibits nuclease-like activity with preferred cleaving sites. The mechanism involves nucleotide-biased adsorption and hydroxyl radical-assisted phosphodiester hydrolysis. Compared with previously reported artificial metallonucleases, the liquid gallium uniquely integrates its oxide layer for substrate adsorption and its metallic core with electrons as a cleavage active center, forming a ligand- and cofactor-free artificial nuclease platform. Moreover, their activity is tunable through synthesis parameters and external stimuli, enabling programmable control with spatial or temporal precision. This work presents a minimalistic yet functional approach to enzyme mimicry, expanding the design space for abiotic enzymatic systems and offering potential opportunities in therapeutic applications, synthetic biology, and biomaterials.

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Cite This Study

Liu et al. (2026) studied this question.

synapsesocial.com/papers/69db37b04fe01fead37c5c81https://doi.org/10.1038/s41467-026-71346-7
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