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<p>Protein coacervates formed by liquid-liquid phase separation are emerging as active force generators, independent of ATP-driven motors. Nevertheless, the coordination and force scaling of protein coacervates remain largely unexplored. Here, we engineer a temperature-responsive elastin-based protocell model displaying temperature-modulated contractility and attendant force harnessing. By leveraging the phase separation properties, we modulate the protocell dynamics associated with volume contraction and membrane budding. Crosslinking of the elastin-based membrane influences the contraction dynamics such that the accumulation of mechanical forces in the protocells results in the spontaneous expulsion of internally trapped protein liquid-liquid phase separation (LLPS) complexes. We use a simple mathematically model to show how protein coacervation can amplify small piconewton-scale forces to perform large-scale mechanical work, highlighting the mechanical potential of protein coacervation dynamics. Taken together, our results provide a model framework for harnessing protein coacervates-driven forces and offer a step to future applications in synthetic biology, biomaterials and next-generation soft robotics.</p>

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Protein coacervation-driven active forces power protocell dynamics

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年4月7日

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  • Haiyang Jia,
  • Huan Sun,
  • Weijie Zhang,
  • Xiao Ning,
  • Stephen Mann

摘要

Protein coacervates formed by liquid-liquid phase separation are emerging as active force generators, independent of ATP-driven motors. Nevertheless, the coordination and force scaling of protein coacervates remain largely unexplored. Here, we engineer a temperature-responsive elastin-based protocell model displaying temperature-modulated contractility and attendant force harnessing. By leveraging the phase separation properties, we modulate the protocell dynamics associated with volume contraction and membrane budding. Crosslinking of the elastin-based membrane influences the contraction dynamics such that the accumulation of mechanical forces in the protocells results in the spontaneous expulsion of internally trapped protein liquid-liquid phase separation (LLPS) complexes. We use a simple mathematically model to show how protein coacervation can amplify small piconewton-scale forces to perform large-scale mechanical work, highlighting the mechanical potential of protein coacervation dynamics. Taken together, our results provide a model framework for harnessing protein coacervates-driven forces and offer a step to future applications in synthetic biology, biomaterials and next-generation soft robotics.