Coding

Part:BBa_K200013

Designed by: James Field   Group: iGEM09_Imperial College London   (2009-10-13)
Revision as of 14:41, 18 October 2009 by JamesField (Talk | contribs)

Opiorphin + EK cleavage site

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

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.

Since polypeptides can only be biologically synthesised if they start with the amino acid methionine, it has been necessary to design a cleavable peptide sequence starting with methionine. This sequence is found upstream of opiorphin and is enzymatically cleaved following incubation with the enzyme enterokinase. Enterokinase is a highly specific serine protease that cleaves after the recognition sequence Aspartic Acid - Aspartic Acid - Aspartic Acid - Aspartic Acid – Lysine.


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]


[edit]
Categories
Parameters
None