Peptide Hormone Powder Dermorphin Best Effect Strong Pain Killer

Dermorphin Basic Info.

Name:Dermorphin
Synonyms:H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser(Ac)-Nh2;h-Tyr-d-Ala-Phe-Gly-Tyr-Pro-Ser-Nh2;(Ser(Ac)7)-Dermorphin;Tyr-d-Ala-Phe-Gly-Tyr-Pro-Ser-Nh2;Yafgyps-Nh2;Dermorphin Acetate Salt
MF:C40H50N8O10
MW:802.87
Solubility:Soluble in water. The contents of this vial have been accurately determined. Both the stopper and the vial have been siliconized. Do not attempt to weight out a smaller portion of the contents. Dermorphin has no common structure with mammalian opioid peptides and is a unique example of a peptide. This peptide is the most selective m-opioid agonist. isolated from the skin of the South American frog Phyllomedusa sauvagei, is the most selective of all m-opioid agonists.
Function:Dermorphin has a very potent opiate-like activity. It has high affinity and selectivity for mu-type opioid receptors (By similarity).

Dermorphin Description

Dermorphin is a hepta-peptide first isolated from the skin of South American frogs belonging to the genus Phyllomedusa. The peptide is a natural opioid that binds as an agonist with high potency and selectivity to mu Opioid receptors. Dermorphin is about 30-40 times more potent than morphine but theoretically may be less likely to produce drug tolerance and addiction (due to its high potency). The amino acid sequence of dermorphin is H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2.
 
Dermorphin is not found in humans or other mammals and similar D-amino acid peptides have only been found in bacteria, amphibians and molluscs. Dermorphin appears to be made in these through an unusual posttranslational modification carried out by an amino acid isomerase. This unusual process is needed because the D-alanine in this peptide is not among the 20 amino acids coded for in the genetic code and thus the peptide cannot be synthesized in the usual way from the encodings in the genome of an organism.