Coding

Part:BBa_K200013

Designed by: James Field   Group: iGEM09_Imperial College London   (2009-10-13)
Revision as of 14:57, 18 October 2009 by JamesField (Talk | contribs)

Opiorphin + EK cleavage site

Usage and Biology

Background

Opiorphin is a pentapeptide (five amino acids long) that was isolated from human saliva in 1996. Opiorphin acts as a pain killing agent. The amino acid sequence for opiorphin is Glutamine-Arginine-Phenylalanine-Serine-Arginine.

Mechanism of Action

Preliminary rat studies indicate that opiorphin has a pain killing effect six times stronger than that of morphine. With regards to its mechanism of action, opiorphin prevents the breakdown of enkephalins which are natural pain-killing opioids.

EK Cleavage

See 'Design Notes' for our rationale behind incorporating an EK cleavage sequence on the N terminus of the opiorphin pentapeptide.


Side Effects

A recent study involved genetically engineering retired breeder rats to constitutively express opiorphin. Interestingly, this resulted in the development of a priapic-like condition. It is thought that this condition resulted from the upregulation of the ornithine decarboxylase gene (ODC) by opiorphin 1.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]



References

<biblio>

  1. 1 pmid=19657052

</biblio>

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