Competitive Advantages
- Able to encapsulate antimicrobial peptides
- Compact, soluble and non-toxic
- Resistant to degradation
Summary
We have developed a method to alter the structure of GFP to serve as storage for proteins of interest in drug delivery. Unlike other modes of delivery, GFPs were shown to be compact, soluble, and non-toxic whilst being resistant to degradation by proteases. Bactenecin, an antimicrobial peptide, was incorporated into GFP, and the GFP-bactenecin structure was stabilized through insertion of point mutations. The optimized protein had no toxic effect on the cells during its production in bacterial culture. Results show that modified GFP can be used as a container for toxic peptides or other non-native proteins for a wide range of therapeutic applications.
Optimized Structure of GFP-Bactenecin with Stabilizing Mutations
Desired Partnerships
- License
- Sponsored Research
- Co-Development