Part:BBa_K200013
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.
References
<biblio>
- 1 pmid=19657052
</biblio>
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
None |