Dermaseptin-PT9 [D8K,E23K] peptide

Dermaseptin-PT9 [D8K,E23K] peptide

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

H-GLWSKIKKAAKTAGKAALGFVNKMV-NH2

H-Gly-Leu-Trp-Ser-Lys-Ile-Lys-Lys-Ala-Ala-Lys-Thr-Ala-Gly-Lys-Ala-Ala-Leu-Gly-Phe-Val-Asn-Lys-Met-Val-NH2

25

95.2%

C₁₂₁H₂₀₆N₃₄O₂₈S

2617.2

Synthetic

Powder

Dermaseptin-PT9 (DPT9) (sequence: GLWSKIKDAAKTAGKAALGFVNEMV-NH₂) is a novel dermaseptin peptide isolated and identified from Phyllomedusa tarsius by the combination of molecular cloning and LC-MS analysis. Chemically synthesised DPT9 was broadly effective against the tested microorganisms through the disruption of cell membranes and showed weak haemolytic activity towards horse erythrocytes. It also exhibited anti-proliferative effect against various human cancer cells. Dermaseptin-PT9 [D8K,E23K] (sequence: GLWSKIKKAAKTAGKAALGFVNKMV-NH₂) is an analoge of DPT9, had a markedly increased antimicrobial effect against all tested microorganisms and disrupted microbial cell membranes. This analogue also showed no haemolysis at its effective antimicrobial concentrations. In addition, Dermaseptin-PT9 [D8K,E23K] displayed an enhanced anti-proliferative effect against cancer cells, while displayed weak activity against the normal human cell line, HMEC-1.

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

• Li M, Xi X, Ma C, et al. A Novel Dermaseptin Isolated from the Skin Secretion of Phyllomedusa tarsius and Its Cationicity-Enhanced Analogue Exhibiting Effective Antimicrobial and Anti-Proliferative Activities. Biomolecules. 2019;9(10)

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.