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◆ Nature Communications2026-04-10· Nuclease

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

原始摘要(英文原文)· Original 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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Gallium in liquid state shows nuclease-mimicking activity — 科研速览 Science Skim