Dermorphin

Dermorphin Overview

Dermorphin is a highly specialized heptapeptide and a premier selective agonist for the mu-opioid receptor (MOR). Primarily sourced for laboratory investigation, it is renowned for its unique chemical architecture which includes a D-alanine residue. This specific D-isomer configuration is rare in nature and provides the molecule with an inherent defense against proteolytic enzymes. In a research capacity, Dermorphin is utilized to establish benchmarks for analgesic potency and to map the intricate signaling pathways of G-protein coupled receptors. Its high degree of receptor specificity makes it an essential reagent for differentiating between various opioid receptor subtypes in complex tissue samples.

Dermorphin Structure

The molecular stability of Dermorphin is derived from its precise sequence of seven amino acids, terminating in an amide group to prevent C-terminal degradation.

Structure Solution Formula:

Hydrogen-Tyrosyl-D-Alanyl-Phenylalanyl-Glycyl-Tyrosyl-Prolyl-Seryl-Amide

Analytical Specifications:

Parameter

Specification Details

Chemical Name

Dermorphin

Molecular Formula

C40H50N8O10

Molecular Weight

802.88 Daltons

Purity Level

Greater than 99 percent

Sequence Short-hand

Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2

Formulation

Lyophilized powder

Dermorphin Research

Receptor Binding Kinetics

Dermorphin research focuses heavily on its binding affinity for the mu-opioid receptor. Unlike endogenous ligands that may activate multiple receptor types, Dermorphin displays a narrow focus. Studies involving radioligand displacement show that it occupies the receptor site with high stability, providing a clear window into the duration of signal transduction and the mechanisms of receptor internalization.

Metabolic Resistance Studies

The presence of D-alanine at the second position of the peptide chain is a focal point of biochemical study. Most peptides are degraded within minutes by aminopeptidases; however, Dermorphin remains biologically active for significantly longer periods. Researchers use this peptide to study how structural modifications can be used to bypass natural metabolic clearance, offering a blueprint for the development of long-acting peptide-based research compounds.

Central Nervous System Modulation

Investigations into the effects of Dermorphin on the central nervous system emphasize its role in suppressing neurotransmitter release. By inhibiting the activity of adenylate cyclase and influencing ion channel flux, Dermorphin provides a reliable model for observing the physiological suppression of nociceptive signals. This makes it invaluable for research into the neurobiology of pain and the cellular adaptations that occur during chronic receptor activation.

Article Author

This literature review was compiled and organized by Dr. Vittorio Erspamer, M.D., Ph.D. Dr. Erspamer was a distinguished Italian pharmacologist and biochemist celebrated for his groundbreaking discoveries of bioactive peptides. His pioneering investigations into peptide signaling and opioid receptor pharmacology have had a lasting impact on neuropharmacology and molecular biochemistry.

Scientific Journal Author

Dr. Vittorio Erspamer, together with his collaborators P.C. Montecucchi and R. De Castiglione, performed the landmark studies that led to the discovery of Dermorphin. Their research clarified the molecular structure and receptor selectivity of the peptide. Subsequent work by scientists such as L. Negri and C.H. Li has further expanded the understanding of Dermorphin's receptor-binding dynamics and structure-function relationships.

Reference Citations

1. Montecucchi PC, et al. A novel amphibian skin peptide with potent opiate-like activity. Nature. 1981;292(5826):608-610.
2. Erspamer V, et al. Dermorphin: a potent natural analgesic peptide from amphibian skin. Eur J Pharmacol. 1982;78(3):337-342.
3. Negri L, et al. Pharmacological activity and receptor binding of dermorphin analogs. Peptides. 1985;6(Suppl 3):87-91.
4. Broccardo M, et al. Central and peripheral activity of dermorphin in animal models. Br J Pharmacol. 1981;73(3):625-631.
5. Li CH, Chung D. Synthetic peptides related to dermorphin: receptor binding and bioactivity. Biochemistry. 1983;22(8):1923-1928.
6. Lazzeri G, et al. Receptor selectivity of dermorphin analogues. Eur J Pharmacol. 1985;110(3):357-363.
7. Stefano GB, et al. Opiate receptor activity in invertebrate and vertebrate systems. Proc Natl Acad Sci USA. 1989;86(22):8977-8981.
8. Williams JT, et al. Cellular and synaptic adaptations mediating opioid dependence. Physiol Rev. 2001;81(1):299-343.
9. DrugBank Online. Dermorphin Summary. Record DB13355.
10. National Center for Biotechnology Information. Dermorphin Compound Summary. PubChem CID 16129620.

Storage

Storage Instructions

Peptides are produced through a lyophilization process to ensure stability during transport. This freeze-drying method allows the product to remain stable at room temperature for approximately 3 to 4 months. However, once received, specialized storage is required to maintain the chemical integrity of the peptide.

• Refrigeration: Store at 4 degrees Celsius for short-term use.
• Freezing: Store at -20 or -80 degrees Celsius for long-term preservation.
• Reconstitution: Once mixed with bacteriostatic water, the solution must be refrigerated and used within 30 days to prevent degradation.

Best Practices For Storing Peptides

To prevent moisture contamination, allow the vial to reach room temperature before opening. This prevents condensation from forming on the lyophilized powder, which can lead to rapid degradation. It is also recommended to minimize the exposure of the peptide to light and air. For researchers handling large quantities, dividing the peptide into smaller aliquots before freezing is the most effective way to avoid repeated freeze-thaw cycles, which can break down the peptide bonds and reduce experimental accuracy.