(118f) Invited Talk: Leveraging Self-Assembly of Recombinant Fusion Proteins to Design Biomimetic Protocells

The living cell could have evolved from a simpler precursor, protocell – a self-assembled particulate where chemical and biological processes take place around or within. We develop a systematic engineering approach to construct a protein-powered synthetic protocell based on the self-assembly of recombinant globular fusion proteins into cellular compartment-like structures. Amphiphilic recombinant fusion proteins made of globular protein, leucine zippers, and elastin-like polypeptide (ELP) self-assemble into coacervates or vesicles depending on environmental conditions. In this talk, I will discuss our understanding of the structural properties of protein vesicles, such as stability upon external stimuli triggers, membrane structures, and permeability, which are critical to integrating and engineering their biological functionalities. Our ongoing work to make giant protein vesicles towards synthetic cells with de novo protein synthesis through in vitro transcription and translation and sensing of biochemicals will also be discussed. Creating a synthetic protocell would provide an understanding of how complex biological cells come from non-living molecules and a powerful practical tool to create sophisticated cellular functions in synthetic materials.