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Fabrication of fibrillosomes from droplets stabilized by protein nanofibrils at all-aqueous interfaces
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Fabrication of fibrillosomes from droplets stabilized by protein nanofibrils at all-aqueous interfaces
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Journal Article
Fabrication of fibrillosomes from droplets stabilized by protein nanofibrils at all-aqueous interfaces
2016
Overview
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.
All-aqueous emulsions are useful for delivering and processing biomolecules, but their stability is constrained by low interfacial adsorption energy. Song
et al
. solve this problem using protein nanofibrils that form a crosslinked network, whose stability is superior to conventional colloidal capsules.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
