Difference between revisions of "Part:BBa K200013"

Revision as of 14:53, 18 October 2009

Opiorphin + EK cleavage site

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.

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]

@@ Line 13: / Line 13: @@
 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.