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Engineering Globular Protein Vesicles through Tunable Self‐Assembly of Recombinant Fusion Proteins
Author(s) -
Jang Yeongseon,
Choi Won Tae,
Heller William T.,
Ke Zunlong,
Wright Elizabeth R.,
Champion Julie A.
Publication year - 2017
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201700399
Subject(s) - globular protein , recombinant dna , vesicle , self assembly , fusion , biophysics , materials science , fusion protein , nanotechnology , lipid bilayer fusion , chemistry , crystallography , membrane , biochemistry , biology , linguistics , philosophy , gene
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.