Abstract
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.
| Original language | English |
|---|---|
| Article number | 1700399 |
| Journal | Small |
| Volume | 13 |
| Issue number | 36 |
| DOIs | |
| State | Published - Sep 27 2017 |
Funding
This research was financially supported by M. T. Campagna. The authors acknowledge Prof. D. Tirrell and Prof. K. Zhang for DNA plasmids. A portion of this research used resources at the Spallation Neutron Source, a DOE Office of Science User Facility operated by the Oak Ridge National Laboratory. This work was performed in part at the Georgia Tech Institute for Electronics and Nanotechnology, a member of the National Nanotechnology Coordinated Infrastructure, which is supported by the National Science Foundation (Grant No. ECCS-1542174). Also, the authors would like to thank the Robert P. Apkarian Integrated Electron Microscopy Core of Emory University for microscopy services and support. This work was supported in part by Emory University; Children's Healthcare of Atlanta; the Georgia Research Alliance; the Center for AIDS Research at Emory University (P30 AI050409); the James B. Pendleton Charitable Trust; Public Health Service Grant Nos. R01GM114561 and R01GM104540; and NSF Grant No. 0923395 to E.R.W.
| Funders | Funder number |
|---|---|
| National Science Foundation | 0923395, ECCS-1542174 |
| National Institute of General Medical Sciences | R01GM114561 |
| Office of Science | |
| Oak Ridge National Laboratory | |
| Emory University | |
| Georgia Research Alliance | |
| Center for AIDS Research, Emory University | P30 AI050409 |
| James B. Pendleton Charitable Trust | R01GM104540 |
| Children's Healthcare of Atlanta |
Keywords
- elastin-like polypeptides
- globular proteins
- protein vesicles
- recombinant fusion proteins
- self-assembly