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Porcine α-Neoendorphin is a 10-residue endogenous prodynorphin-derived opioid peptide with the sequence Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro-Lys.
It contains an N-terminal Leu-enkephalin motif followed by a basic C-terminal extension that contributes to the distinctive κ-opioid pharmacology of prodynorphin-derived ligands.
Product Information
| Property | Specification |
|---|---|
| Product Name | α-Neo-Endorphin, Porcine |
| Catalog No. | AS2590 |
| Sequence | Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro-Lys |
| One-Letter Sequence | YGGFLRKYPK |
| Peptide Length | 10 residues |
| Molecular Formula | C60H89N15O13 |
| Molecular Weight | Approximately 1228.4 Da |
| Precursor | Prodynorphin |
| Research Focus | κ-opioid signaling and prodynorphin processing |
The Full α-Neoendorphin Sequence
Unlike the 1-7 and 1-8 fragments, the native decapeptide retains Tyr8-Pro9-Lys10. The terminal lysine contributes to the strongly basic character of the molecule and forms part of the extended receptor-address region found in κ-active prodynorphin peptides.
κ-Opioid Receptor Research
Classical receptor studies characterized α-Neoendorphin as a strong κ-opioid agonist, and later human receptor experiments showed that it can behave as a potent full agonist at the κ receptor.
Its receptor pharmacology should still be interpreted in the context of assay system and peptide concentration because endogenous opioid peptides are not always absolutely subtype-selective.
Prodynorphin Processing
α-Neoendorphin, β-Neoendorphin and dynorphin peptides arise from the same precursor family but differ in their C-terminal extensions. Comparing these products can help map how precursor processing changes receptor profile and protease susceptibility.
Related truncations can be prepared through our Chemical Peptide Synthesis capabilities.
Frequently Asked Questions
How many residues are in α-Neoendorphin?
The full α-Neoendorphin peptide contains 10 amino-acid residues.
Which precursor produces α-Neoendorphin?
It is generated from prodynorphin.