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

Jang, Yeongseon; Choi, Won Tae; Heller, William T.; Ke, Zunlong; Wright, Elizabeth R.; Champion, Julie A.

doi:10.1002/smll.201700399

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

Journal Article · Thu Jul 27 00:00:00 EDT 2017 · Small

DOI:https://doi.org/10.1002/smll.201700399· OSTI ID:1399972

Jang, Yeongseon ^[1]; Choi, Won Tae ^[1]; ^[2]; Ke, Zunlong ^[3]; Wright, Elizabeth R. ^[4]; Champion, Julie A. ^[1]

Georgia Inst. of Technology, Atlanta, GA (United States)
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Emory Univ. School of Medicine, Children's Healthcare of Atlanta, Atlanta, GA (United States); Georgia Inst. of Technology, Atlanta, GA (United States)
Emory Univ. School of Medicine, Children's Healthcare of Atlanta, Atlanta, GA (United States)

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. Lastly, these results provide critical information to engineer globular protein vesicles via self-assembly with desired size and membrane structure.

View Accepted Manuscript (DOE)

Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 1399972

Journal Information:: Small, Journal Name: Small Journal Issue: 36 Vol. 13; ISSN 1613-6810

Publisher:: WileyCopyright Statement

Country of Publication:: United States

Language:: English

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Complex microparticle architectures from stimuli-responsive intrinsically disordered proteins Roberts, Stefan; Miao, Vincent; Costa, Simone Nature Communications, Vol. 11, Issue 1 https://doi.org/10.1038/s41467-020-15128-9	journal	March 2020
Engineering the Architecture of Elastin‐Like Polypeptides: From Unimers to Hierarchical Self‐Assembly Saha, Soumen; Banskota, Samagya; Roberts, Stefan Advanced Therapeutics, Vol. 3, Issue 3 https://doi.org/10.1002/adtp.201900164	journal	February 2020
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36 MATERIALS SCIENCE
60 APPLIED LIFE SCIENCES
elastin-like polypeptides
globular proteins
protein vesicles
recombinant fusion proteins
self-assembly

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

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