CF-14 peptide

CF-14 peptide

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

Batch to batch variation of the purity

H-RIVELTLPRVSVRL-NH2

H-Arg-Ile-Val-Glu-Leu-Thr-Leu-Pro-Arg-Val-Ser-Val-Arg-Leu-NH2

14

95.2%

C₇₄H₁₃₆N₂₄O₁₈

1650.01

Synthetic

Powder

CF-14(RIVELTLPRVSVRL-NH2) is a novel antibacterial peptide, derived from the epidermal mucus of catfish. CF-14 showed antibacterial activity against S. putrefaciens and S. aureus, as well as Escherichia coli compared to negative controls. When the concentration of CF-14 was 62.5 μg/mL, the antibacterial effect of CF-14 against S. putrefaciens was similar to that of 50 μg/mL of ampicillin. CF-14 displays potent activity against gram-negative (S. putrefaciens) bacteria and gram-positive bacteria (S. aureus). Further, the MIC of CF-14 against S. putrefaciens was 62.5 μg/mL. The antimicrobial activity of CF-14 showed no obvious change after heat treatment for 30 min at either at 40 °C, 60 °C, or 80 °C, and slight inactivation after treatment at 100 °C for 30 min. CF-14 remained stable after 24 h after exposure to a pH values ranging from 4.0 to 12.0, but the antimicrobial activity of CF-14 decreased after exposure to an acidic environment (pH < 4). Finally, CF-14 was susceptible to proteases as no antimicrobial activity was observed after treatment with trypsin, pepsin, or proteinase K. CF-14 has the ability to enhance the membrane permeability of S. putrefaciens. Moreover, observations performed using scanning electron and confocal microscopy indicated that CF-14 could penetrate into the cell membranes of S. putrefaciens and accumulate in bacterial cells, but did not break down cell membranes. Further, electrophoresis analysis demonstrated that CF-14 possesses DNA-binding affinity.

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

• Li T, Liu Q, Wang D, Li J. Characterization and antimicrobial mechanism of CF-14, a new antimicrobial peptide from the epidermal mucus of catfish. Fish Shellfish Immunol. 2019

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.