Epinecidin-1 peptide

Epinecidin-1 peptide

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

GFIFHIIKGLFHAGKMIHGLV

H-Gly-Phe-Ile-Phe-His-Ile-Ile-Lys-Gly-Leu-Phe-His-Ala-Gly-Lys-Met-Ile-His-Gly-Leu-Val-NH2

21

95.5%

C₁₁₄H₁₇₆N₃₀O₂₁S

2334.91

Synthetic

Powder

Epinecidin-1 is an antimicrobial peptide with antitumor and antiviral activity. It corresponds to positions 22-42 of the grouper (Epinephelus coioides) epinecidin-1 and shows structural homology to pleurocidin found in the winter flounder (Pleuronectes americanus). The synthetic peptide Epinecidin-1 has the potential to serve as a therapeutic drug for use against bacterial infectious diseases. It also showed antiviral activity against non-enveloped, spherical virus (betanodavirus) (Wang Y et al. 2010 Peptides 31: 1026-33). It showed efficacy in the animal model:zebrafish (Pan CY et al 2011 Fish Shellfish Immunol online Sep 10, in press). Animal model:mouse: Epi-1 can reduce MRSA bacterial counts in the wounded region, promote wound healing, and increase angiogenesis at the injury site. Epi-1 treatment decreaseds the proinflammatory cytokines TNF-?, IL-6, and MCP-1 in the serum, and regulated the recruitment of monocytes and clearance of lymphocytes around the wounded region during healing (Huang HN et al., 2013). Updated 9/20/11; sequence 10/7/2013. The source of Epinecidin-1 is orange-spotted grouper, Epinephelus coioides.

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

• Z.X.Yin et al., Aquaculture, 253, 204 (2006)
• C.Y.Pan et al., DNA Cell Biol., 26, 403 (2007)
• J.Y.Chen et al., Peptides, 30, 2365 (2009)
• C.Y.Pan et al., Peptides, 30, 1058 (2009)
• W.J.Lin et al., Peptides, 30, 283 (2009)
• C.Y.Pan et al., Peptides, 31, 806 (2010)
• T.J.Chia et al., Fish Shellfish Immunol., 28, 434 (2010)
• Y.D.Wang et al., Fish Shellfish Immunol., 28, 113 (2010)

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.