RANATUERIN 3 peptide

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

Batch to batch variation of the purity

Ranatuerins are a family of antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. Nine peptides, designated ranatuerins 1 through 9, were purified from an extract of adult bullfrog skin and characterized. These peptides are structurally diverse: ranatuerins 1 and 4 contain an intramolecular disulfide bridge that forms a heptapeptide ring, while ranatuerins 2 and 3 feature a disulfide bridge forming a hexapeptide ring. Ranatuerins 5 through 9 are shorter peptides comprising 12 to 14 amino acids and show sequence similarity to the hemolytic peptides A1 and B9 previously isolated from the skin of Rana esculenta.

Ranatuerrin 1 (sequence: SMLSVLKNLGKVGLGFVACKINKQC) exhibits the broadest spectrum of antimicrobial activity among the peptides, inhibiting the growth of Staphylococcus aureus, Escherichia coli, and the yeast Candida albicans. Structural analysis predicts that ranatuerins 2, 3, and 4 contain a single amphipathic alpha-helix, while ranatuerin 1 possesses two alpha-helical regions joined by a glycine-containing hinge, a conformation resembling that of cecropin-family antimicrobial peptides. Ranatuerins 5 through 8 are predicted to contain a single alpha-helical region, whereas ranatuerin 9 is predicted to adopt either a random coil or a beta-sheet structure.

• Goraya J, Knoop FC, Conlon JM. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. Biochem Biophys Res Commun. 1998;250(3):589-92.
• Mechkarska M, Ojo OO, Meetani MA, Coquet L, Jouenne T, Abdel-Wahab YH, Flatt PR, King JD, Conlon JM. Peptidomic analysis of skin secretions from the bullfrog Lithobates catesbeianus (Ranidae) identifies multiple peptides with potent insulin-releasing activity. Peptides. 2011 Feb;32(2):203-8.

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.