Mimicking Dividing Cells by Assembly of Protein Structures Inside Aqueous Two-Phase Droplets

Abstract

In this work, we demonstrate that assembly of macromolecules, such as proteins, can cause aqueous droplets to exhibit division, even in the absence of a cell membrane. The all-aqueous nature of the systems results in tunable interfacial tension, affinity partitioning and osmotic responses. The solubility of different types of macromolecules across the interfaces enables new strategies to assemble structures at the droplet interfaces. While the significantly lower interfacial tension can make stabilization of the interface difficult due to the slow adsorption dynamics by surfactants and particles, structures that have been assembled at the interfaces can be easily expelled. This contributes to the more sophisticated dynamics of the hierarhically structured all-aqueous droplets. These droplets have great potential to be utilized as templates for fabricating materials with novel properties.