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Liquid-liquid phase separation-boosted transmembrane delivery in interactive protocell communities
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Liquid-liquid phase separation-boosted transmembrane delivery in interactive protocell communities
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Journal Article
Liquid-liquid phase separation-boosted transmembrane delivery in interactive protocell communities
2025
Overview
Stress stimulation-mediated liquid-liquid phase separation is a key activity in living organisms, but its biophysical characteristics are poorly understood. Here, we report a UV-light stress stimulation behaviour in a binary community of synthetic protocells of condensates and proteinosomes, showing that condensates could behave like Condensate Pumps to enable a stepwise controlled transmembrane mass transfer regardless of the permeability barrier of proteinosomes. The stimulation mechanism of interfacial tension-induced proteinosome deformation and transient high osmotic pressure arisen by the dissociation of condensate is proposed. Accordingly, under UV-light stress stimulation, unexpected characteristics could be triggered by transmembrane pumping oversized biomacromolecules into proteinosomes including liquid-liquid reentrant phase separation, DNA unwinding, and protein synthesis. Therefore, our results not only reveal unique physical principles and potential characteristics of macromolecular assemblies at droplet-membrane interface but also highlight a pathway for transmembrane transport of biomacromolecules which is anticipated to serve as a powerful technique to inducing higher-order behaviour in synthetic protocells community.
Stress stimulation-mediated liquid-liquid phase separation is an essential feature of living organisms, but its biophysical characteristics are poorly understood. Here, the authors report a UV-light stress stimulation behaviour in a binary community of synthetic protocells of condensates and proteinosomes, showing that condensates could behave like condensate pumps to enable a stepwise controlled transmembrane mass transfer regardless of the permeability barrier of proteinosomes.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
