Achatin I peptide

Achatin I peptide

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

Batch to batch variation of the purity

H-GFAD-OH

H-Gly-Phe-Ala-Asp-OH

4

95.11%

C₁₈H₂₄N₄O₇

408.4

Synthetic

Powder

Achatin I is an endogenous neuroexcitatory tetrapeptide purified from the suboesophageal and cerebral ganglia of the African giant snail Achatinafulica Ferussac. The amino acid sequence of Achatin I is Gly-D-Phe-Ala-Asp.
Achatin I induced a voltage-dependent inward current, due to Na +, on the identifiable giant neuron, periodically oscillating neuron (PON), of the same snail. The sensitivity of the neuron to Achatin I and its isomers was strictly stereospecific; among the various isomers, only Achatin I showed marked effects (ED50 = 2.29 x 10-6 M), while Gly-D-Phe-D-Ala-Asp, the synthetic D-Ala-isomer, was less than 10-3 active.

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

• Kamatani Y, Minakata H, Kenny PT, et al. Achatin-I, an endogenous neuroexcitatory tetrapeptide from Achatina fulica Férussac containing a D-amino acid residue. Biochem Biophys Res Commun. 1989;160(3):1015-20.

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.