Temporin [K3]SHa peptide

Temporin [K3]SHa peptide

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

Batch to batch variation of the purity

H-FLKGIVGMLGKLF-NH2

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

13

95.41%

C₇₀H₁₁₆N₁₆O₁₃S

1421.83

Synthetic

Powder

Temporin [K3]SHa is a synthetic peptide analog of temporin-SHa (SHa). It was designed to improve the antibacterial and antiparasitic activity of SHa. [K3]SHa exhibits potent activity against a wide range of bacteria (MIC = 1 - 6 μM for most tested bacteria), yeasts/fungi (MIC = 3 - 25 μM), and trypanosomatids (Leishmania and Trypanosoma). It is also effective against antibiotic-resistant strains of S. aureus and antimony-resistant L. infantum. [K3]SHa is significantly more active than the parent peptide SHa, especially against Gram-negative bacteria and yeasts/fungi. For example, the MIC values decreased by approximately 8-fold for P. aeruginosa, 4-fold for S. enterica, and 3-fold for E. coli. [K3]SHa also has potent and rapid antiprotozoal activities against different species of Leishmania (responsible for visceral, cutaneous, and mucocutaneous leishmaniases) and Trypanosoma (T. brucei gambiense and T. cruzi).

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

• Raja Z, André S, Abbassi F, Humblot V, Lequin O, Bouceba T, Correia I, Casale S, Foulon T, Sereno D, Oury B, Ladram A. Insight into the mechanism of action of temporin-SHa, a new broad-spectrum antiparasitic and antibacterial agent. PLoS One. 2017 Mar 20;12(3):e0174024. doi: 10.1371/journal.pone.0174024. PMID: 28319176; PMCID: PMC5358776.

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.