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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
Published on: April 8, 2020
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Protein Vesicles Self-Assembled from Functional Globular Proteins with Different Charge and Size
Dylan R Dautel1, Julie A Champion1
1School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 950 Atlantic Drive NW, Atlanta, Georgia 30332, United States.
Biomacromolecules
|September 4, 2020
Summary
Researchers created functional protein vesicles by altering globular protein size and charge. Larger globular proteins yielded smaller, more stable vesicles, paving the way for biocatalysis and drug delivery applications.
Area of Science:
- Biotechnology
- Materials Science
- Protein Engineering
Background:
- Protein vesicles are synthesized using fusion proteins like elastin-like polypeptide (ELP) and leucine zippers (ZR and ZE).
- Current applications are limited to fluorescent proteins; broader utility requires incorporating diverse functional proteins.
Purpose of the Study:
- To investigate the impact of globular protein surface charge and size on protein vesicle self-assembly.
- To establish phase diagrams for vesicle formation with different globular proteins.
- To demonstrate the potential of protein vesicles for biocatalysis and biosensing.
Main Methods:
- Systematic modification of the globular protein component in fusion proteins.
- Monitoring microphase formation (vesicles, coacervates, hybrid structures) under varying assembly conditions.
- Characterization of vesicle size and stability in relation to protein properties and molar ratios.
Main Results:
- Protein surface charge had a minimal effect on vesicle self-assembly.
- Increased globular protein size led to smaller vesicle dimensions.
- Larger globular proteins enhanced vesicle stability at lower ZE/ZR molar ratios.
- Catalytically active enzyme vesicles were successfully synthesized.
Conclusions:
- Phase diagrams provide guidelines for incorporating new functional proteins into vesicles.
- Protein vesicle size and stability are tunable by modifying the globular protein component.
- The development of functional enzyme vesicles opens avenues for biocatalysis and biosensing applications.
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