Multiphase protein microgels

Peptides and proteins represent attractive building blocks for the development of new functional materials due to the biocompatibility and biodegradability of many naturally abundant proteins. In nature, sophisticated material functionality is commonly achieved through spatial control of protein localisation and structure on both the nano and micro scales. We approached this requirement in an artificial setting by exploiting the propensity of proteins to self-assemble into amyloid fibrils to achieve nano scale order, and utilised aqueous liquid/liquid phase separation to control the micron scale localization of the proteinaceous component under microconfinement. We show that in combination with droplet microfluidics, this strategy allows the synthesis of core-shell microgel particles composed of protein nanofibrils. It shown that the characteristics of aqueous two-phase systems can be exploited in combination with protein self-assembly for controlling aggregation and structuring of fibrillar proteins into 3D core-shell microgels.