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

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.
Authors:
 [1] ;  [1] ; ORCiD logo [2] ;  [3] ;  [4] ;  [1]
  1. Georgia Inst. of Technology, Atlanta, GA (United States)
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  3. Emory Univ. School of Medicine, Children's Healthcare of Atlanta, Atlanta, GA (United States); Georgia Inst. of Technology, Atlanta, GA (United States)
  4. Emory Univ. School of Medicine, Children's Healthcare of Atlanta, Atlanta, GA (United States)
Publication Date:
Grant/Contract Number:
AC05-00OR22725
Type:
Accepted Manuscript
Journal Name:
Small
Additional Journal Information:
Journal Volume: 13; Journal Issue: 36; Journal ID: ISSN 1613-6810
Publisher:
Wiley
Research Org:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org:
USDOE Office of Science (SC)
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; 60 APPLIED LIFE SCIENCES; elastin-like polypeptides; globular proteins; protein vesicles; recombinant fusion proteins; self-assembly
OSTI Identifier:
1399972

Jang, Yeongseon, Choi, Won Tae, Heller, William T., Ke, Zunlong, Wright, Elizabeth R., and Champion, Julie A.. Engineering Globular Protein Vesicles through Tunable Self-Assembly of Recombinant Fusion Proteins. United States: N. p., Web. doi:10.1002/smll.201700399.
Jang, Yeongseon, Choi, Won Tae, Heller, William T., Ke, Zunlong, Wright, Elizabeth R., & Champion, Julie A.. Engineering Globular Protein Vesicles through Tunable Self-Assembly of Recombinant Fusion Proteins. United States. doi:10.1002/smll.201700399.
Jang, Yeongseon, Choi, Won Tae, Heller, William T., Ke, Zunlong, Wright, Elizabeth R., and Champion, Julie A.. 2017. "Engineering Globular Protein Vesicles through Tunable Self-Assembly of Recombinant Fusion Proteins". United States. doi:10.1002/smll.201700399. https://www.osti.gov/servlets/purl/1399972.
@article{osti_1399972,
title = {Engineering Globular Protein Vesicles through Tunable Self-Assembly of Recombinant Fusion Proteins},
author = {Jang, Yeongseon and Choi, Won Tae and Heller, William T. and Ke, Zunlong and Wright, Elizabeth R. and Champion, Julie A.},
abstractNote = {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.},
doi = {10.1002/smll.201700399},
journal = {Small},
number = 36,
volume = 13,
place = {United States},
year = {2017},
month = {7}
}