Gallium in liquid state shows nuclease-mimicking activity

Nat Commun. 2026 Apr 10;17(1):5126. doi: 10.1038/s41467-026-71346-7.

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.

MeSH terms

  • Adsorption
  • Deoxyribonucleases* / chemistry
  • Deoxyribonucleases* / metabolism
  • Gallium* / chemistry
  • Hydrolysis
  • Hydroxyl Radical / chemistry

Substances

  • Gallium
  • Hydroxyl Radical
  • Deoxyribonucleases