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5 years ago

Engineering Globular Protein Vesicles through Tunable Self-Assembly of Recombinant Fusion Proteins

Engineering Globular Protein Vesicles through Tunable Self-Assembly of Recombinant Fusion Proteins
Julie A. Champion, Won Tae Choi, Yeongseon Jang, Elizabeth R. Wright, William T. Heller, Zunlong Ke
Vesicles assembled from folded, globular proteins have potential for functions different from traditional lipid or polymeric vesicles. However, they also present challenges in understanding the assembly process and controlling vesicle properties. From detailed investigation of the assembly behavior of recombinant fusion proteins, this work reports a simple strategy to engineer protein vesicles containing functional, globular domains. This is achieved through tunable self-assembly of recombinant globular fusion proteins containing leucine zippers and elastin-like polypeptides. The fusion proteins form complexes in solution via high affinity binding of the zippers, and transition through dynamic coacervates to stable hollow vesicles upon warming. The thermal driving force, which can be tuned by protein concentration or temperature, controls both vesicle size and whether vesicles are single or bi-layered. These results provide critical information to engineer globular protein vesicles via self-assembly with desired size and membrane structure. Globular protein vesicles are self-assembled from globule-zipper-elastin-like polypeptide (ELP) protein complexes upon warming. The vesicle self-assembly proceeds according to the packing parameter of the fusion protein complexes, which depends on the ELP domain phase. The size and membrane structure of the globular protein vesicles are engineered by tuning the molecular packing parameter via protein concentration or temperature.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/smll.201700399

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