Budding-like division of all-aqueous emulsion droplets modulated by networks of protein nanofibrils

Yang Song, Thomas C. T. Michaels, Qingming Ma, Zhou Liu, Hao Yuan, Shuichi Takayama, Tuomas P. J. Knowles, Ho Cheung Shum*

*Corresponding author for this work

Research output: Journal Publications and ReviewsRGC 21 - Publication in refereed journalpeer-review

91 Citations (Scopus)
11 Downloads (CityUHK Scholars)

Abstract

Networks of natural protein nanofibrils, such as cytoskeletal filaments, control the shape and the division of cells, yet mimicking this functionality in a synthetic setting has proved challenging. Here, we demonstrate that artificial networks of protein nanofibrils can induce controlled deformation and division of all-aqueous emulsion droplets with budding-like morphologies. We show that this process is driven by the difference in the immersional wetting energy of the nanofibril network, and that both the size and the number of the daughter droplets formed during division can be controlled by modulating the fibril concentration and the chemical properties of the fibril network. Our results demonstrate a route for achieving biomimetic division with synthetic self-assembling fibrils and offer an engineered approach to regulate the morphology of protein gels. © 2018 The Author(s).
Original languageEnglish
Article number2110
JournalNature Communications
Volume9
Issue number1
DOIs
Publication statusPublished - 1 Dec 2018
Externally publishedYes

Bibliographical note

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Funding

We are very grateful to Professor Michael Cates (Cambridge) and Professor L. Mahadevan (Harvard) for helpful discussions and for input into the theoretical analysis. This research was supported by the Early Career Scheme (HKU 707712P), the General Research Fund (HKU 719813E, 17304514, and 17306315) and the Collaborative Research Fund (C6004-14G) from the Research Grants Council of Hong Kong, the Major Research Plan (91434202) and the General Program (21476189/B060201) from the National Natural Science Foundation of China, the National Science Foundation of USA (IIP1456281), the Swiss National Science Foundation (T.C.T.M.), Peterhouse Cambridge (T.C.T.M.), the European Research Council under the European Union’s Seventh Framework Program (FP7/2007-2013) through the ERC grant PhysProt (agreement no 337969), the Wellcome Trust (T.P.J.K.) and the Frances and Augustus Newman Foundation (T.P.J.K.).

Publisher's Copyright Statement

  • This full text is made available under CC-BY 4.0. https://creativecommons.org/licenses/by/4.0/

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