title: Fabrication of fibrillosomes from droplets stabilized by protein nanofibrils at all-aqueous interfaces.
abstract: 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.
authors.affiliation: Department of Mechanical Engineering, the University of Hong Kong, Pokfulam Road, Hong Kong.|Institute for Research and Innovation (HKU-SIRI), Shenzhen 518000, China.
authors.forename: Yang
authors.initials: Y
authors.lastname: Song
authors.affiliation: Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.|Department of Materials and Interfaces, Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Ulyana
authors.initials: U
authors.lastname: Shimanovich
authors.affiliation: Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.|Paulson School of Engineering and Applied Science, Harvard University, Cambridge, Massachusetts 02138, USA.
authors.forename: Thomas C T
authors.initials: TC
authors.lastname: Michaels
authors.affiliation: Department of Mechanical Engineering, the University of Hong Kong, Pokfulam Road, Hong Kong.|Institute for Research and Innovation (HKU-SIRI), Shenzhen 518000, China.
authors.forename: Qingming
authors.initials: Q
authors.lastname: Ma
authors.affiliation: Department of Mechanical Engineering, the University of Hong Kong, Pokfulam Road, Hong Kong.|Institute for Research and Innovation (HKU-SIRI), Shenzhen 518000, China.
authors.forename: Jingmei
authors.initials: J
authors.lastname: Li
authors.affiliation: Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
authors.forename: Tuomas P J
authors.initials: TP
authors.lastname: Knowles
authors.affiliation: Department of Mechanical Engineering, the University of Hong Kong, Pokfulam Road, Hong Kong.|Institute for Research and Innovation (HKU-SIRI), Shenzhen 518000, China.
authors.forename: Ho Cheung
authors.initials: HC
authors.lastname: Shum
mesh_terms: D000682:Amyloid / Q000737:chemistry; D000818:Animals; D002645:Chickens; D004655:Emulsions / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D057139:Nanofibers / Q000737:chemistry* / Q000648:ultrastructure; D011092:Polyethylene Glycols / Q000737:chemistry; D066329:Protein Aggregates; D013499:Surface Properties; D014867:Water / Q000737:chemistry*
chemical_list: D000682:Amyloid; D004655:Emulsions; D066329:Protein Aggregates; D014867:Water; D011092:Polyethylene Glycols; D009113:Muramidase