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Regulatory

Eledoisin: Mollusk Undecapeptide with Vasodilator Power

Eledoisin, an undecapeptide from mollusk salivary glands, acts as a potent vasodilator and smooth muscle contractor. Isolated in 1975 from Eledone species, it belongs to the tachykinin family and binds to NK-1, NK-2, and NK-3 receptors. Research highlights its potential in treating dry eyes and links to Alzheimer's progression through sequence similarity to beta-amyloid fragments.

Marcus Hopkin, PhD, Director of Research and Development at Volta Peptides.

Reviewed by Marcus Hopkin, PhD

Director of Research and Development, Volta Peptides

Written by Volta Peptides Editorial Team · Reviewed September 15, 2026

May 12, 2026Updated June 19, 20263 min read

Key Takeaways

  • •Researchers first isolated eledoisin in 1975 from the posterior salivary glands of two mollusk species, Eledone moschata and Eledone, both in the octopod order of Cephalopoda.
  • •Eledoisin qualifies as an undecapeptide derived from mollusks.
  • •Scientists often use it as a vasodilator.

Eledoisin: Mollusk Undecapeptide with Vasodilator Power

Researchers first isolated eledoisin in 1975 from the posterior salivary glands of two mollusk species, Eledone moschata and Eledone, both in the octopod order of Cephalopoda. De Marco and Gatti conducted this separation. This compound serves as a key member of the tachykinin family of neuropeptides.

Origins and Basic Properties

Eledoisin qualifies as an undecapeptide derived from mollusks. Its molecular weight stands at 1188.4 Da. The amino acid sequence reads pGlu-Pro-Ser-Lys-Asp-Ala-Phe-Ile-Gly-Leu-Met-NH2, with a molecular formula of C54H85N13O15S.

Scientists often use it as a vasodilator. It also contracts extravascular smooth muscle. For detailed peptide properties, check the Peptide Glossary.

Receptor Binding Profile

This tachykinin from amphibians and mollusks interacts with the same three sites that bind mammalian tachykinins or neurokinins: substance P, neurokinin A, and neurokinin B. These sites are known as NK-1, NK-2, and NK-3. The eledoisin-preferring SPE receptor likely consists of mixtures of these binding sites.

Experts no longer view SPE as a distinct neurokinin site. This stems from eledoisin's low selectivity for mammalian receptors. Such properties arise from its binding characteristics.

Pharmacological Activities

Like other nonmammalian tachykinins such as kassinin and physalaemin, eledoisin shows a broad range of effects. It causes strong vasodilation and hypertensive action. It also stimulates extravascular smooth muscle.

Its pharmacological patterns result from combined receptor stimulation across cell types in tissues. NK-3 sites appear only on postganglionic cholinergic neurons. NK-2 sites reside solely on smooth muscle cells, while NK-1 sites occur on both neurons and smooth muscle cells.

Use tools like the Half-Life Calculator or Stability Calculator for research on similar compounds.

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Potential Medical Applications

Studies suggest eledoisin holds promise in Alzheimer's disease onset and progression. This links to its activity and 73% sequence homology with beta-amyloid protein fragments Ab 25, 35 and their analogs. These fragments play a major role in the condition.

Recent work has applied eledoisin successfully to treat dry eyes. Comprehensive reports on its pharmacology and metabolism remain limited. For peptide research planning, visit Free peptide tools.

Structural and Membrane Interactions

Eledoisin does not interact with lipid membranes when water is present. It adopts a β-structure upon contact with phosphatidylcholine membranes. This change may result from peptide aggregation.

Detailed studies confirm these traits through various methods. Solution structure analysis appears in biophysical research. Conformation studies use NMR and CD spectroscopy.

Key Research References

  1. Grace, R. C. R., Chandrashekar, I. R., & Cowsik, S. M. (2003). Solution structure of the tachykinin peptide eledoisin. Biophysical journal, 84(1), 655-664.
  1. Sanz-Nebot, V., Toro, I., & Barbosa, J. (1999). Fractionation and characterization of a crude peptide mixture from the synthesis of eledoisin by liquid chromatography-electrospray ionization mass spectrometry. Journal of Chromatography A, 846(1-2), 25-38.
  1. Lippe, C., Bellantuono, V., Ardizzone, C., & Cassano, G. (2004). Eledoisin and Kassinin, but not Enterokassinin, stimulate ion transport in frog skin. Peptides, 25(11), 1971-1975.
  1. Nebbioso, M., Evangelista, M., Librando, A., Plateroti, A. M., & Pescosolido, N. (2013). Iatrogenic dry eye disease: an eledoisin/carnitine and osmolyte drops study. Biomedicine & Pharmacotherapy, 67(7), 659-663.
  1. Wilson, J. C., Nielsen, K. J., McLeish, M. J., & Craik, D. J. (1994). A determination of the solution conformation of the nonmammalian tachykinin eledoisin by NMR and CD spectroscopy. Biochemistry, 33(22), 6802-6811.
  1. Schwyzer, R. (1987). Membrane-assisted molecular mechanism of neurokinin receptor subtype selection. The EMBO journal, 6(8), 2255-2259.

Eledoisin continues to draw interest for its tachykinin properties and diverse biological roles. Ongoing studies may clarify its full therapeutic potential. Researchers can explore more via Latest peptide news.

Research Use Only. This article is provided for informational and educational purposes only. The compounds and topics discussed are intended solely for laboratory and scientific research. This content does not constitute medical advice, and Volta Peptides does not endorse or promote human consumption of any research compound.

About the reviewer

Marcus Hopkin, PhD, Director of Research and Development at Volta Peptides.

Marcus Hopkin, PhD

Director of Research and Development, Volta Peptides

Marcus Hopkin, PhD, is Director of Research and Development at Volta Peptides. He has more than 12 years of analytical chemistry experience, including direct laboratory work in peptide synthesis, characterization, purity testing and stability assessment. His doctoral research at the University of Michigan examined novel peptide structures in the human proteome and their potential significance for therapeutic-peptide research. Before joining Volta Peptides he held research and development roles at Amgen and Eli Lilly and Company, and served as a lecturer at the University of Michigan.

Marcus reviewed this article for scientific and analytical accuracy on September 15, 2026. He did not write it. Technical review is internal review and is not peer review, independent third-party review or medical review.

Disclosure. Marcus Hopkin is an employee of Volta Peptides and serves as its Director of Research and Development. Volta Peptides sells research compounds related to subjects discussed in the content he writes and reviews. His reviews are internal scientific and technical review and must not be described as independent third-party review, peer review or medical review.

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