Eledoisin peptide

Eledoisin peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

Pyr-PSKDAFIGLM-NH2

Pyr-Pro-Ser-Lys-Asp-Ala-Phe-Ile-Gly-Leu-Met-NH2

10

95.82%

C₅₄H₈₅N₁₃O₁₅S

1188.39

69-25-0

10328936

Synthetic

Powder

Eledoisin is a peptide that comes from the salivary glands of the octopod Eledone moschata. It has been used in experimentation for a long time as it was available in pure form before the structures of Substance P, Neurokinin A, and Neurokinin B were elucidated. In mammals, Eledoisin is a specific agonist of NK3 receptors. In frog skin, it stimulates ion transport, as estimated by measuring the short-circuit current (SCC) value. The stimulation of SCC by Eledoisin is reduced by CP99994 (a NK1 antagonist) and SR48968 (a NK2 antagonist), but not affected by SB222200 (a NK3 antagonist). The C-terminal pentapeptide of Eledoisin is Phe-X-Gly-Leu-Met-NH₂, and it has an Asp in position 7 from the C-terminus and an Ile in position 4. These characteristics make it different from other tachykinins. Overall, Eledoisin plays a role in the stimulation of ion transport in frog skin, and its pharmacological profile is different from that of other tachykinins.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Lippe C, Bellantuono V, Ardizzone C, Cassano G. Eledoisin and Kassinin, but not Enterokassinin, stimulate ion transport in frog skin. Peptides. 2004 Nov;25(11):1971-5. doi: 10.1016/j.peptides.2004.06.014. PMID: 15501529.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.