Deltorphins, Dermorphins and Analogs
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Deltorphins, Dermorphins and Analogs

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Cat. # Product Name Price
D03018 H-Tyr-D-Ala-Phe-Trp-Asn-NH2· TFA Inquiry
D03017 H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Lys-NH2 Inquiry
D03008 Dermorphin Inquiry
D03016 Deltorphin II Inquiry
D03015 Deltorphin I Inquiry
D03005 Deltorphin C Inquiry
D03004 Deltorphin B Inquiry
D03003 Deltorphin A Inquiry
D03014 (Ser(Ac)7)-Dermorphin Inquiry
D03011 (Phe4)-Dermorphin (1-4) amide Inquiry
D03007 (Met2)-Deltorphin Inquiry
D03013 (D-Arg2,Sar4)-Dermorphin (1-4) Inquiry
D03006 (D-Arg2,Lys4)-Dermorphin (1-4) amide Inquiry
D03012 (D-Arg2)-Dermorphin (1-4) amide Inquiry

Introduction of Deltorphins Analogs

Deltorphin, also known as deltorphin A and dermenkephalin, is a naturally occurring exogenous opioid heptapeptide with an amino acid sequence of Tyr-D-Met-Phe-Leu-Met-Asp-NH2. Together with other Deltofen (such as deltorphin I and deltorphin II) and dermatins, Deltorphin is an endogenous component of leaf frogs such as Phyllomedusa, P.bicolor and P.sauvagei where it is produced in their skin, but it is not known that it exists naturally in their skin. Deltorphin is one of the highest affinity and most selective natural opioid peptides known. It is a very effective and highly specific agonist of δ-opioid receptor.

Introduction of Dermorphins Analogs

Demorphine is a kind of heptapeptide isolated from the skin of South American frog for the first time. It belongs to Mucor (Phyllomedusa). This peptide is a natural opioid, which can bind to μ opioid receptor as an agonist and has high potency and selectivity. The potency of demorphine is 30 to 40 times that of morphine, but it is unlikely to be produced in theory. The amino acid sequence of demorphine is H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2. Demorphine does not exist in humans or other mammals, while similar D-amino acid peptides are found only in bacteria, amphibians and molluscs. Demorphine seems to be produced by an unusual post-translation modification of amino acid isomerases. This unusual process is necessary because the D-alanine in this peptide is not one of the 20 amino acids encoded in the genetic code and therefore not a peptide, which can’t be synthesized from the coding of the genome of an organism in the usual way.


The current opioid crisis has created a tragic problem in medicine and society. Pain is the most common and expensive disease in society, but all our “treatments” are toxic, especially for long-term use. However, in the past 15 years, several alternative drugs have been found in animals, proving that they do not have the toxicity of current drugs. Demoxine is a selective μ-opioid receptor agonist. It was isolated from the skin extract of frogs belonging to the genus Phyllomedusa and has been shown to bring pain back to life in patients with postoperative pain syndrome. Studies have shown that intracerebroventricular injection of demoxine can produce a lasting antinociceptive effect, which is more than 200 times more effective than morphine. In the future, researchers should continue to conduct in-depth research in this direction and develop more analgesic drugs.

1. Mizusawa, K. (2016). Dermorphin. In Handbook of Hormones (pp. 64-65). Academic Press.
2. Hruby, V. J. (2019). Multivalent Peptide and Peptidomimetic Ligands for the Treatment of Pain without Toxicities and Addiction. Peptides.

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