Dermorphin peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

Dermorphin is a heptapeptide isolated from methanol extracts of the skin of the South American frog Phyllomedusa sauvagei. Its amino acid sequence is H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH₂. This peptide exhibits potent opiate-like activity and is structurally distinct from known enkephalins. A notable feature is the presence of a D-alanine residue at position 2, which is rare among vertebrate peptides and crucial for its biological properties.

The isolation and structural analysis of dermorphin involved techniques such as gel filtration, silica gel chromatography, and enzymatic digestions. The peptide's resistance to certain proteolytic enzymes contrasts with the rapid degradation of typical enkephalins. Studies confirm that the D-alanine configuration is inherent to the natural peptide and not an artifact of isolation, suggesting a specialized biosynthetic origin.

• Montecucchi PC, De castiglione R, Piani S, Gozzini L, Erspamer V. Amino acid composition and sequence of dermorphin, a novel opiate-like peptide from the skin of Phyllomedusa sauvagei. Int J Pept Protein Res. 1981;17(3):275-83.

Trifluoroacetic acid (TFA) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.