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) 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.