Temporin-1CEa peptide

Temporin-1CEa peptide

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

Batch to batch variation of the purity

FVDLKKIANIINSIFGK

Phe-Val-Asp-Leu-Lys-Lys-Ile-Ala-Asn-Ile-Ile-Asn-Ser-Ile-Phe-Gly-Lys

17

95.5%

Synthetic

Powder

Shang D et al (2009) reported previously "Molecular cloning of cDNAs encoding antimicrobial peptide precursors from the skin of the Chinese brown frog, Rana chensinensis" (Zoolog Sci. 2009 Mar;26(3):220-6). Temporin-1CEa adopted a well-defined helical structure in 50% TFE/water solution. It appears to kill breast cancer cells by membrane disruption Wang C et al., 2013. APD update 7/14/12; 4/12/13 GW. Temporin-1CEa has Antibacterial, Anticancer activity. Temporin-1CEa was found in Asia, Chinese brown frog, Rana chensinensis.

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

• Wang C, Li HB, Li S, Tian LL, Shang DJ. Antitumor effects and cell selectivity of temporin-1CEa, an antimicrobial peptide from the skin secretions of the Chinese brown frog (Rana chensinensis). Biochimie. 2012;94(2):434-41.

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.