Phylloseptin-L2 peptide

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

Batch to batch variation of the purity

Phylloseptin-L2 is a peptide belonging to the phylloseptin family, isolated from the skin secretions of the Lemur leaf frog Hylomantis lemur, a species within the Phyllomedusinae subfamily. Its primary structure, FLSLIPHVISALSSL, was determined through automated Edman degradation, and the peptide is C-terminally alpha-amidated. Phylloseptin-L2 exhibits the ability to stimulate insulin release from rat clonal BRIN-BD11 beta cells in a concentration-dependent manner, with a significant effect observed at 30 nM and a maximum response at 3 µM, without compromising plasma membrane integrity as indicated by the lack of lactate dehydrogenase release.

The peptide’s insulinotropic action appears to be independent of extracellular calcium influx and ATP-sensitive potassium channel closure, as activity is maintained in the absence of calcium and in the presence of verapamil and diazoxide. Phylloseptin-L2 has low cationicity, which is inversely related to its antimicrobial potency, suggesting a mechanism of action that involves traversing the plasma membrane without permeabilization. The peptide is structurally related to other phylloseptins found in Phyllomedusa species but lacks a basic residue, influencing its reduced antimicrobial activity while enhancing its insulin-releasing properties.

• Yasser H.A. Abdel-Wahab; Gavin J. Power; Peter R. Flatt; Douglas C. Woodhams; Louise A. Rollins-Smith; J. Michael Conlon. (2008). A peptide of the phylloseptin family from the skin of the frog Hylomantis lemur (Phyllomedusinae) with potent in vitro and in vivo insulin-releasing activity. 29(12), 0–2143.

Trifluoroacetic acid (TFA) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.