Skh-AMP1 peptide

Skh-AMP1 peptide

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

Batch to batch variation of the purity

H-GRTSKQELCTWERGSVRQADKTIAG-NH2

H-Gly-Arg-Thr-Ser-Lys-Gln-Glu-Leu-Cys-Thr-Trp-Glu-Arg-Gly-Ser-Val-Arg-Gln-Ala-Asp-Lys-Thr-Ile-Ala-Gly-NH2

25

95.2%

C₁₁₅H₁₉₄N₄₀O₃₈S

2777.07

Synthetic

Powder

Skh-AMP1 is an antifungal peptide isolated from Satureja khuzistanica which has been shown to have strong antifungal activity against Aspergillus and Candida species, but no obvious hemolytic effects or cell cytotoxicity in vitro. In the present study, Skh-AMP1 was synthesized, and its mode of action on the plasma membrane, mitochondria, and morphological and ultrastructural changes against conidia and hyphae of Aspergillus fumigatus were evaluated. The results indicated that Skh-AMP1 had sporicidal activities against the non-germinated conidia of A. fumigatus at concentrations of 40 and 80 muM. Skh-AMP1 induced the release of K(+) and the uptake of propidium iodide and enhanced reactive oxygen species (ROS) production in the conidia and hyphae of the fungus. Scanning and transmission electron microscopy showed deformation and shrinkage of the hyphae and conidia, cell membrane disruption and detachment from the cell wall, microvesicle formation, vacuolation and depletion of cytoplasm and organelles of the hyphae of A. fumigatus exposed to 40-80 muM of the peptide. The results further demonstrated that the antifungal activity of Skh-AMP1 may be related to its ability to disrupt fungal cell membrane permeabilization and induce enhanced ROS production. Therefore, Skh-AMP1 can be introduced as a novel antifungal candidate for developing new therapeutic agents.

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

• Khani S, Seyedjavadi SS, Zare-Zardini H, et al. Isolation and functional characterization of an antifungal hydrophilic peptide, Skh-AMP1, derived from Satureja khuzistanica leaves. Phytochemistry. 2019;164:136u2013143. doi:10.1016/j.phytochem.2019.05.011

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.