Cecropin A peptide

Cecropin A peptide

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

Batch to batch variation of the purity

H-KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK-NH2

H-Lys-Trp-Lys-Leu-Phe-Lys-Lys-Ile-Glu-Lys-Val-Gly-Gln-Asn-Ile-Arg-Asp-Gly-Ile-Ile-Lys-Ala-Gly-Pro-Ala-Val-Ala-Val-Val-Gly-Gln-Ala-Thr-Gln-Ile-Ala-Lys-NH2

37

95.02%

C₁₈₄H₃₁₃N₅₃O₄₆

4003.76

Synthetic

Powder

Cecropin A (CeA) is a natural linear cationic α-helical antimicrobial peptide (AMP) originally identified in moths (Hyalophora cecropia) and later in pig intestine. Cecropin A contains a strongly cationic region at its N-terminus and a large hydrophobic tail at its C-terminus, which allow its interaction with the microbial membrane, and then cell lysis by pore formation. Cecropin A has a wide spectrum of antimicrobial activities against gram-negative bacteria, gram-positive bacteria, and fungal phytopathogens. Cecropins constitute a main part of the innate immune system of insects.

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

• Kulagina et al (2007) Antimicrobial peptides as new recognition molecules for screening challenging species. Sens. Actuators B Chem. 121(1) 150 PMID: 18231571
• Yu et al (2016) Combination Effects of Antimicrobial Peptides. Antimicrob. Agents and Chemother. 60 (3) 1717 PMID: 26729502

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.