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Frog-derived opioid heptapeptide; D-Ala selective mu-receptor agonist
Overview
Dermorphin is a heptapeptide opioid, first characterized in 1981 by Montecucchi and colleagues from skin secretions of Phyllomedusa sauvagei, the South American waxy monkey leaf frog. It holds a distinctive place in peptide chemistry as the first vertebrate peptide shown to incorporate a D-amino acid: the D-alanine at position two both shields the backbone from peptidase attack and imparts markedly high affinity and selectivity for the mu-opioid receptor. These properties make it a standard probe in opioid-receptor pharmacology, analgesic-mechanism investigation, and the design of new analgesic candidates. Lyochem supplies Dermorphin as a lyophilized reference standard to a ≥99.0% HPLC purity specification, with the C40H50N8O10 composition confirmed by ESI-MS against the ~802.9 Da mass on the batch COA, and the D-Ala-containing sequence can be walked out by LC-MS/MS peptide mapping on request. RP-HPLC establishes main-peak purity while resolving any epimeric or deletion species; residual counter-ion and water content are available on request so the reported quantity can be expressed as net peptide.
Applications & buyer fit
Cognitive and neuropeptide buyers are predominantly research labs running in vivo rodent studies. The dominant administration route in the published literature is intranasal — Semax, Selank, DSIP, Pinealon — because these peptides are not meaningfully blood-brain-barrier permeable when delivered systemically. For in vivo workflows, endotoxin and microbial-limit testing is recommended at the CoA stage so the bioassay readout is not confounded by contamination unrelated to the test article.
Academic Laboratories
Universities, medical schools, and government research institutes qualifying a reference standard for a method-development or in vivo workflow.
Biotech R&D Groups
Preclinical biotech and pharmaceutical discovery teams sourcing characterized peptides for receptor-pharmacology, screening, and method-development campaigns.
Every lot has its own batch-specific CoA — HPLC purity and MS identity, plus any analytical scope agreed at quote stage — tied to the exact lot you receive.
Review a representative batch CoA before you order, so you can confirm the packet matches what your method or sponsor audit needs.
Supplied strictly as a research reagent to research institutions — not a finished dosage form and not for human administration. Buyer qualification runs at the inquiry stage.
Specifications
Documentation available on request
Regulatory note
Supplied by Lyochem strictly for controlled in-vitro research and analytical reference work. This peptide is not authorized for human or veterinary administration, nor for any diagnostic, therapeutic, or non-laboratory use.
Selected literature
Frequently asked questions
The position-two D-residue is the defining structural feature, so RP-HPLC is run under conditions that separate the D-Ala peptide from its all-L epimer, which would otherwise be a near-mass-identical contaminant that ESI-MS alone cannot distinguish. LC-MS/MS peptide mapping, available on request, confirms residue order, and the resolved chromatographic purity is reported on every batch COA.
We ship the material lyophilized and advise reconstitution in an appropriate buffer immediately before use to limit backbone hydrolysis in solution. Aliquot to minimize freeze-thaw cycling, hold stock frozen and working dilutions cold, and re-confirm by RP-HPLC if solution-state material has been stored before a quantitative run.
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