Journal
NATURE COMMUNICATIONS
Volume 7, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms12934
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Funding
- Research Grants Council of Hong Kong [HKU 707712P, HKU 719813E, 17304514]
- National Natural Science Foundation of China [21476189/B060201, NSFC51206138/E0605]
- University of Hong Kong [201211159090, 201311159105, 201309160035]
- Doris Zimmern HKU-Cambridge Hughes Hall Fellowship
- BBSRC [BB/J002119/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/J002119/1] Funding Source: researchfish
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All-aqueous emulsions exploit spontaneous liquid-liquid separation and due to their water-based nature are particular advantageous for the biocompatible storage and processing of biomacromolecules. However, the ultralow interfacial tensions characteristic of all-aqueous interfaces represent an inherent limitation to the use of thermally adsorbed particles to achieve emulsion stability. Here, we use protein nanofibrils to generate colloidosome-like two-dimensional crosslinked networks of nanostructures templated by all-aqueous emulsions, which we term fibrillosomes. We show that this approach not only allows us to operate below the thermal limit at ultra-low surface tensions but also yields structures that are stable even in the complete absence of an interface. Moreover, we show that the growth and multilayer deposition of fibrils allows us to control the thickness of the capsule shells. These results open up the possibility of stabilizing aqueous two-phase systems using natural proteins, and creating self-standing protein capsules without the requirement for three-phase emulsions or water/oil interfaces.
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