Recent progress in the chemical construction of colloidal objects comprising integrated biomimetic functions is paving the way towards rudimentary forms of artificial cell-like entities (protocells). Although several new types of protocells are currently available, the design of synthetic protocell communities and investigation of their collective behaviour has received little attention. Here we demonstrate an artificial form of predatory behaviour in a community of protease-containing coacervate microdroplets and protein-polymer microcapsules (proteinosomes) that interact via electrostatic binding. The coacervate microdroplets act as killer protocells for the obliteration of the target proteinosome population by protease-induced lysis of the protein-polymer membrane. As a consequence, the proteinosome payload (dextran, single-stranded DNA, platinum nanoparticles) is trafficked into the attached coacervate microdroplets, which are then released as functionally modified killer protocells capable of rekilling. Our results highlight opportunities for the development of interacting artificial protocell communities, and provide a strategy for inducing collective behaviour in soft matter microcompartmentalized systems and synthetic protocell consortia.
The integration of molecularly crowded microenvironments into membrane‐enclosed protocell models represents a step towards more realistic representations of cellular structure and organization. Herein, the membrane diffusion‐mediated nucleation of either negatively or positively charged coacervate microdroplets within the aqueous lumen of individual proteinosomes is used to prepare nested hybrid protocells with spatially organized and chemically coupled enzyme activities. The location and reconfiguration of the entrapped droplets are regulated by tuning the electrostatic interactions between the encapsulated coacervate and surrounding negatively charged proteinosome membrane. As a consequence, alternative modes of a cascade reaction involving membrane‐ and coacervate‐segregated enzymes can be implemented within the coacervate‐in‐proteinosome protocells.
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.
The oxime connection between linear peptides and hydrophobic aldehydes affords amphiphiles that are excellent biocompatible scaffolds for the hierarchical self-assembly of nano and micro fibrillar structures in aqueous media.
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