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Eledoisin is an undecapeptide of mollusk origin and it belongs to the tachykinin family of neuropeptides. It was first isolated from the posterior salivary glands of two mollusk species Eledone muschata and Eledone aldovandi. Eledoisin has the amino acid sequence pGlu-Pro-Ser-Lys-Asp-Ala-Phe-Ile-Gly-Leu-Met-NH2. It is the Potent natural tachykinin receptor ligand.

Peptide Inhibitors
Catalog number
CAS number
Molecular Formula
Molecular Weight
(3S)-3-[[(2S)-6-amino-2-[[(2S)-3-hydroxy-2-[[(2S)-1-[(2S)-5-oxopyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]propanoyl]amino]hexanoyl]amino]-4-[[(2S)-1-[[(2S)-1-[[(2S,3S)-1-[[2-[[(2S)-1-[[(2S)-1-amino-4-methylsulfanyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-3-methyl-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoic acid
Eledone peptide; Eledoisinum; 5-oxo-L-prolyl-L-prolyl-L-seryl-L-lysyl-L-α-aspartyl-L-alanyl-L-phenylalanyl-L-isoleucylglycyl-L-leucyl-L-methioninamide
White lyophilised solid
1.289 g/cm3
Boiling Point
1618.1±65.0°C at 760 mmHg
Store at -20°C
Soluble in DMSO
Neurotransmitter Agents
InChI Key
Canonical SMILES
1.Structural heterogeneity of doubly-charged peptide b-ions.
Li X1, Huang Y, O'Connor PB, Lin C. J Am Soc Mass Spectrom. 2011 Feb;22(2):245-54. doi: 10.1007/s13361-010-0036-1. Epub 2011 Jan 29.
Performing collisionally activated dissociation (CAD) and electron capture dissociation (ECD) in tandem has shown great promise in providing comprehensive sequence information that was otherwise unobtainable by using either fragmentation method alone or in duet. However, the general applicability of this MS(3) approach in peptide sequencing may be undermined by the formation of non-direct sequence ions, as sometimes observed under CAD, particularly when multiple stages of CAD are involved. In this study, varied-sized doubly-charged b-ions from three tachykinin peptides were investigated by ECD. Sequence scrambling was observed in ECD of all b-ions from neurokinin A (HKTDSFVGLM-NH(2)), suggesting the presence of N- and C-termini linked macro-cyclic conformers. On the contrary, none of the b-ions from eledoisin (pEPSKDAFIGLM-NH(2)) produced non-direct sequence ions under ECD, as it does not contain a free N-terminal amino group. ECD of several b-ions from Substance P (RPKPQQFFGLM-NH(2)) showed series of c(m)-Lys fragment ions which suggested that the macro-cyclic structure may also be formed by connecting the C-terminal carbonyl group and the ε-amino group of the lysine side chain.
2.Characterization of receptors for two Xenopus gastrointestinal tachykinin peptides in their species of origin.
Johansson A1, Liu L, Holmgren S, Burcher E. Naunyn Schmiedebergs Arch Pharmacol. 2004 Jul;370(1):35-45. Epub 2004 Jul 2.
Two tachykinin peptides, bufokinin and Xenopus neurokinin A (X-NKA) were recently isolated from Xenopus laevis. In this study we investigated the tachykinin receptors in the Xenopus gastrointestinal tract. In functional studies using stomach circular muscle strips, all peptides had similar potencies (EC50 values 1-7 nM). The rank order of potency to contract the intestine was physalaemin (EC50 1 nM)> or =bufokinin (EC50 3 nM)>substance P (SP)> or =cod SP>NKA>>X-NKA (EC50 1,900 nM). No maximum response could be obtained for [Sar9,Met(O2)11]SP, eledoisin and kassinin. In stomach strips, the mammalian tachykinin receptor antagonists RP 67580 (NK1) and MEN 10376 (NK2) had agonistic effects but did not antagonize bufokinin or X-NKA. In intestinal strips, RP 67580 (1 microM) reduced the maximal response to X-NKA but not bufokinin, while MEN 10376 was ineffective. [125I]BH-bufokinin bound with high affinity to a single class of sites, of KD 213+/-35 (stomach) and 172+/-9.
3.Eledoisin and Kassinin, but not Enterokassinin, stimulate ion transport in frog skin.
Lippe C1, Bellantuono V, Ardizzone C, Cassano G. Peptides. 2004 Nov;25(11):1971-5.
In frog skin, tachykinins stimulate the ion transport, estimated by measuring the short-circuit current (SCC) value, by interacting with NK1-like receptors. In this paper we show that Kassinin (NK2 preferring in mammals) increases the SCC, while Enterokassinin has no effect. Therefore, either 2 Pro residues or 1 Pro and 1 basic amino acid must be present in the part exceeding the C-terminal pentapeptide. Eledoisin (NK3 preferring in mammals) stimulation of SCC is reduced by CP99994 and SR48968 (NK1 and NK2 antagonists) and not affected by SB222200 (NK3 antagonist). None of the three antagonists affects Kassinin stimulation of SCC.
4.Iatrogenic dry eye disease: an eledoisin/carnitine and osmolyte drops study.
Nebbioso M1, Evangelista M, Librando A, Plateroti AM, Pescosolido N. Biomed Pharmacother. 2013 Sep;67(7):659-63. doi: 10.1016/j.biopha.2013.07.001. Epub 2013 Jul 12.
BACKGROUND: To evaluate the effects of an eye drop containing eledoisin and carnitine in patients suffering from primary open-angle glaucoma (POAG) and ocular discomfort syndrome secondary to a chronically treated with eye drops containing benzalkonium chloride (BAK) as preservative. The dry eye disease was defined as a multifactorial drop disease concerning tears and ocular surface, which brings to discomfort symptoms and visual disorders with potential damage to the ocular surface. Several studies underlined the beneficial effects of secretagogues drugs, such as eledoisin. It is a neuro-peptide extracted from the salivary glands of some shellfishes. Recently, it has been also showed the protective role of carnitine in respect of the ocular surface exposed to the tear film hyperosmolarity.
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