Antagonistic chemical coupling in self-reconfigurable host–guest protocells

Nicolas Martin, Jean-Paul Douliez, Yan Qiao, Richard Booth, Mei Li, Stephen Mann*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

74 Citations (Scopus)
390 Downloads (Pure)


Fabrication of compartmentalised chemical systems with nested architectures and biomimetic properties has important implications for controlling the positional assembly of functional components, spatiotemporal regulation of enzyme cascades and modelling of proto-organelle behaviour in synthetic protocells. Here, we describe the spontaneous capture of glucose oxidase-containing proteinosomes in pH-sensitive fatty acid micelle coacervate droplets as a facile route to multi-compartmentalised host–guest protocells capable of antagonistic chemical and structural coupling. The nested system functions co-operatively at low-substrate turnover, while high levels of glucose give rise to pH-induced disassembly of the droplets, release of the incarcerated proteinosomes and self-reconfiguration into spatially organised enzymatically active vesicle-in-proteinosome protocells. Co-encapsulation of antagonistic enzymes within the proteinosomes produces a sequence of self-induced capture and host–guest reconfiguration. Taken together, our results highlight opportunities for the fabrication of self-reconfigurable host–guest protocells and provide a step towards the development of protocell populations exhibiting both synergistic and antagonistic modes of interaction.

Original languageEnglish
Article number3652
Number of pages12
JournalNature Communications
Publication statusPublished - 7 Sept 2018

Structured keywords

  • BrisSynBio
  • Bristol BioDesign Institute


  • Synthetic Biology


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