Equine β-Endorphin is a 31-residue POMC-derived opioid peptide from horse. Its sequence is closely related to other mammalian β-Endorphins but contains a distinctive serine at position 6, immediately following the conserved N-terminal Met-enkephalin motif.

This natural substitution provides a useful model for investigating how a small change near the opioid pharmacophore influences peptide behavior while leaving most of the extended sequence unchanged.

Product Information

Ser6 Distinguishes the Equine Sequence

Human, rat, camel and porcine β-Endorphins typically contain Thr6. The equine peptide instead contains Ser at this position.

Because both residues are polar hydroxyl-containing amino acids, the substitution is chemically conservative, yet it changes side-chain size and local hydrogen-bonding potential immediately adjacent to the Met-enkephalin domain.

A Natural Structure–Activity Probe

Equine β-Endorphin provides a way to investigate local sequence variation without introducing an artificial mutation. It can be compared with Thr6-containing mammalian peptides in receptor binding, peptide stability or analytical retention studies.

Research Applications

Potential applications include equine neuroendocrine research, opioid receptor studies, natural-sequence SAR and comparative POMC peptide analysis.

Custom β-Endorphin variants can be evaluated through Chemical Peptide Synthesis.

Frequently Asked Questions

What is the main sequence difference in equine β-Endorphin?

A notable difference is Ser6, whereas many other mammalian β-Endorphins contain Thr6.

Is the peptide C-terminally amidated?

No. The listed equine β-Endorphin terminates in Gln with a free carboxyl group.

Research Use Only.