Team:Imperial College London/M1/Opiorphin

From 2009.igem.org


Opiorphin

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Short chain polypeptides have many applications in the field of biopharmaceuticals. Probems arise int he fact that it is difficult to isolate these short chain peptides without the amino acid methionine as the first amino acid in the chain (due to the nature in which DNA is translated into protein, see here for details). As a result these short chain peptides can be difficult and expensive to synthesise and purify.

Opiorphin is a good example of a short chain peptide that encounters these difficulties, and we have chosen it to showcase the possibilies of peptide delivery by The E.ncapsulator. Opiorphin is a pentapeptide (five amino acid sequence) that is naturally produced within the body, and plays a role in pain relief, and as an anti-depressant. The pain killing properties of the chemical are as strong as morphine, although due it's mechanism of action, without the addictive and psychological side effects that come with the more traditional drug. Opiorphin works by inhibiting the production of an enzyme involved in the breakdown of endorphins within the body. By inhibiting the action of this enzyme, endorphins stay present for longer, bringing about the pain relief associated with these molecules.

Unfortunately the chemical is not widely available on the market due to high production costs. We therefore propose the unique peptide synthesis mechanisms of The E.ncapsulator as a synthesis and delivery platform for the drug. We have included a His tag as part of the removable linker mechanism. This allows for easy purification of the compound.



References

Picture from Wikimedia Commons