Scholarlink

<p>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.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Gallium in liquid state shows nuclease-mimicking activity

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年4月10日

查看全文
  • 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

摘要

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.