Gallium in liquid state shows nuclease-mimicking activity
- Li Liu
- Jiewei Zheng
- Xi Lu
- Chowdhury Sarowar
- Yuqin Wang
- Martin A. Smith
- Xin Wang
- Fei Deng
- Biswaranjan Mohanty
- Nur-Adania Nor-Azman
- Fusheng Zhang
- Shih-Hao Chiu
- Mario Torrado
- Yi Li
- Shi-Yang Tang
- Jianbo Tang
- Michelle J. S. Spencer
- Priyank V. Kumar
- Kourosh Kalantar-Zadeh
- Chengchen Zhang
2026-04-10
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.