Dermaseptin-L1 peptide

Dermaseptin-L1 peptide

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

Batch to batch variation of the purity

GLWSKIKEAAKAAGKAALNAVTGLVNQGDQPS

Gly-Leu-Trp-Ser-Lys-Ile-Lys-Glu-Ala-Ala-Lys-Ala-Ala-Gly-Lys-Ala-Ala-Leu-Asn-Ala-Val-Thr-Gly-Leu-Val-Asn-Gln-Gly-Asp-Gln-Pro-Ser

32

95.8%

Synthetic

Powder

Dermaseptin-L1 was active against the Gram-negative bacterium E. coli (MIC=8 uM) but inactive against the Gram-positive bacterium S. aureus. This peptide inhibited growth of zoospores of the chytrid fungus B. dendrobatidis at concentrations above 25 uM but did not completely inhibit growth at 100 uM. Dermaseptin-L1 showed selective cytolytic activity against HepG2 human hepatoma-derived cells (LC50=45 uM) compared with human erythrocytes (LC50=200 uM). Dermaseptin-L1 has Antibacterial, Antifungal activity. Dermaseptin-L1 was found in Hylomantis lemur (Hylidae: Phyllomedusinae).

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

• Conlon JM, Woodhams DC, Raza H, et al. Peptides with differential cytolytic activity from skin secretions of the lemur leaf frog Hylomantis lemur (Hylidae: Phyllomedusinae). Toxicon. 2007;50(4):498-506.

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.