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[1] Target Expression Vector produces fusion protein of interest.
[2] Secretion Tag on fusion protein is recognized by secretion system and transported to extracellular space.
[3] Nano-Tag on fusion protein is recognized by protein on cell surface and binds non-covalently to cell.
[4] Competing binder for surface protein releases protein of interest into supernatant.
The use of recombinant protein production using E. coli-based expression
systems has revolutionized the fields of biotechnology and medicine.
However, the ability to utilize such proteins hinges upon their capacity to
be isolated from their expression systems. Our project aims to create an
all-in-one protein expression and purification system using BioBrick
standards to greatly simplify protein production for synthetic biologists,
reducing the time and cost involved in standard protein purification
methods. Our method uses a novel combination of two systems: secretion and
display. By fusing two tags to the protein it can be secreted into the
expression media, and subsequently directed to bind to the outside of the
cell. To collect the pure proteins, cells only need to be spun down and
then resuspended in an elution buffer, releasing the protein of interest.
Our research exhibits the utility of synthetic biology for developing new
techniques that improve upon established practices.
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