Ascaphin-8 peptide

Ascaphin-8 peptide

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

Batch to batch variation of the purity

GFKDLLKGAAKALVKTVLF

H-Gly-Phe-Lys-Asp-Leu-Leu-Lys-Gly-Ala-Ala-Lys-Ala-Leu-Val-Lys-Thr-Val-Leu-Phe-NH2

19

95.5%

C₉₇H₁₆₄N₂₄O₂₂

2018.4

Synthetic

Powder

Also active against MRSA USA300 (MIC 3.1 uM) (Menousek J et al 2012 Int J Antimicrob Agents 39:402). CD was measured in the presence and absence of TFE. A change of residue 18 to K18 led to an improved TI (Chem Bio Drug Des 2008; 72: 58-64). The peptide is also HIV active (EC50=1.2 uM) (Wang G et al. 2010 Antimicrob. Agents Chemother. 54: 1343-1346). Ascaphin-8 has Antibacterial, Antifungal activity. The source of Ascaphin-8 is Coastal Tailed Frog, Ascaphus truei, Pacific Northwest, USA, North America.

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

• Conlon JM, Sonnevend A, Davidson C, Smith DD, Nielsen PF. The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei. Biochem Biophys Res Commun. 2004;320(1):170-5.

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.