cecropin-4 AMP peptide

cecropin-4 AMP peptide

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

Batch to batch variation of the purity

H-GWLKKKIGKKKIERVGQNTRDATIQAIGVAQQQAANVAATLKGK-OH

H-Gly-Trp-Leu-Lys-Lys-Lys-Ile-Gly-Lys-Lys-Lys-Ile-Glu-Arg-Val-Gly-Gln-Asn-Thr-Arg-Asp-Ala-Thr-Ile-Gln-Ala-Ile-Gly-Val-Ala-Gln-Gln-Gln-Ala-Ala-Asn-Val-Ala-Ala-Thr-Leu-Lys-Gly-Lys-OH

44

95.68%

C₂₀₇H₃₆₀N₆₆O₅₉

4717.46

Synthetic

Powder

Cec4 is a polypeptide with significant antimicrobial properties. It exhibits good antimicrobial activity against gram-negative bacteria, particularly A. baumannii. Cec4 can effectively remove the biofilm formed by carbapenem-resistant A. baumannii, which is a major concern in clinical settings due to its high resistance to antibiotics. This polypeptide is short-chain and amphiphilic, with a net positive charge on its peptide chains. This unique property enables it to bind easily to the negatively charged bacterial membranes, thereby inhibiting bacterial growth and initiating bactericidal action. Cec4 may act on bacteria through multiple mechanisms, such as interfering with cellular signaling systems, inhibiting the alarm system to prevent bacterial overreactivity, suppressing RNA synthesis, and downregulating the expression of binding protein transporter genes responsible for biofilm formation. Overall, Cec4 shows great potential as an antimicrobial agent in the fight against drug-resistant bacteria.

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

• OmpH is Involved in the Decrease of Acinetobacter baumannii Biofilm by the Antimicrobial Peptide Cec4. Drug Design, Development and Therapy. 2024 Dec 7; 2024:18 5795—5810. doi: 10.2147/DDDT.S481225

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.