Morphiceptin peptide

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

Batch to batch variation of the purity

Morphiceptin is a synthetic tetrapeptide with the amino acid sequence NH₂-Tyr-Pro-Phe-Pro-CONH₂. It is derived from a fragment of the milk protein β-casein. This peptide exhibits potent and selective binding affinity for morphine (μ) opiate receptors, with an affinity for μ receptors that is at least 1000 times greater than its affinity for enkephalin (δ) receptors. In bioassays using the guinea pig ileum, morphiceptin demonstrates agonist activity with a potency comparable to morphine, while showing significantly reduced activity in the mouse vas deferens preparation. The peptide's high specificity for μ receptors, along with its resistance to peptidase degradation, makes it a valuable tool for investigating the physiological functions and biochemical properties of opiate receptor subtypes.

• Chang KJ, Lillian A, Hazum E, Cuatrecasas P, Chang JK. Morphiceptin (NH4-tyr-pro-phe-pro-COHN2): a potent and specific agonist for morphine (mu) receptors. Science. 1981 Apr 3;212(4490):75-7. doi: 10.1126/science.6259732. PMID: 6259732.

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.