
Buy Dermorphin Research Peptide
Dermorphin is available as a lyophilised powder, independently HPLC and MS-UPLC tested to ≥98% purity.

Buy Dermorphin Research Peptide
Dermorphin is available as a lyophilised powder, independently HPLC and MS-UPLC tested to ≥98% purity.
HPLC Verified
≥98% purity
Lyophilised
Powder format
Express Shipping
Cold-chain included
COA Available
Every batch
HPLC Verified
≥98% purity
Lyophilised
Powder format
Express Shipping
Cold-chain included
COA Available
Every batch
Same or Next Day Dispatch
Order before 12pm GMT for same-day dispatch; after 12pm ships next business day
Same or Next Day Dispatch
Order before 12pm GMT for same-day dispatch; after 12pm ships next business day
What is Dermorphin?
A synthetic seven-amino-acid opioid peptide first isolated from South American tree frog skin, Dermorphin is studied as a highly selective mu-opioid receptor agonist. Research focuses on its strong selectivity for the mu-opioid receptor and a rare D-alanine residue central to its activity.
- Studied for its high selectivity for the mu-opioid receptor.
- Investigated for the role of its rare D-alanine residue in receptor binding.
- Examined as a research tool for opioid-receptor pharmacology.
- Used in animal models to study mu-opioid receptor signalling.
For research use only. Not intended for human use.
Originally isolated from the skin secretions of South American phyllomedusine frogs, Dermorphin is a naturally occurring heptapeptide and one of the first known examples of a D-amino acid-containing peptide in a vertebrate organism. Also designated Dermorphin natural heptapeptide (CAS 77614-16-5), carries the molecular formula C40H51N7O10 and a molecular weight of 785.88 g/mol. Its sequence Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2 features a D-alanine at position 2. Produced via solid-phase peptide synthesis and is a highly selective mu-opioid receptor agonist.
In vitro radioligand displacement assays using membrane preparations expressing MOR, DOR and KOR have characterised the binding selectivity ratios of Dermorphin across the three classical opioid receptor subtypes. In vivo rodent models have explored the enzymatic stability of the D-Ala2-containing sequence relative to L-Ala2 substituted analogues, examining how the stereochemical inversion at position 2 influences aminopeptidase resistance.
Manufactured in a quality-controlled laboratory to a guaranteed purity of 98% or above. Every batch undergoes independent third-party testing using HPLC and MS-UPLC analysis before dispatch. Vials are vacuum sealed and stored in a temperature-controlled, monitored cold storage system. A batch-specific Certificate of Analysis is available on request.
Sold strictly for in vitro research purposes only. Not for human consumption. Intended for use by qualified researchers in laboratory settings only.
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Quality Guaranteed
Every batch is HPLC-tested to ≥98% purity. Certificate of Analysis and SDS available on request.
