Cm-CATH2 peptide

Cm-CATH2 peptide

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

H-RRSRFGRFFKKVRKQLGRVLRHSRITVGGRMRF-OH

H-Arg-Arg-Ser-Arg-Phe-Gly-Arg-Phe-Phe-Lys-Lys-Val-Arg-Lys-Gln-Leu-Gly-Arg-Val-Leu-Arg-His-Ser-Arg-Ile-Thr-Val-Gly-Gly-Arg-Met-Arg-Phe-OH

33

95.2%

C₁₈₁H₃₀₇N₆₉O₃₈S

4089.86

Synthetic

Powder

Cm-CATH2 is novel cathelicidin identified from green sea turtle. Cm-CATH2, exhibited potent, broad-spectrum and rapid bactericidal and anti-biofilm activities by inducing the disruption of cell membrane integrity. Additionally, Cm-CATH2 effectively induced the macrophages/monocytes and neutrophils trafficking to the infection site, and inhibited the LPS-induced production of inflammatory cytokines, by blocking TLR4/MD2 complex and the downstream signaling pathway activation. In mouse peritonitis and pneumonia models, Cm-CATH2 exhibited evident protection against drugresistant bacterial infections. Cm-CATH2 comprises an α-helix and two β-strands. Cm-CATH2 showed strong and broad-spectrum antimicrobial activity against almost all tested microorganisms, including clinically isolated Gram-positive bacteria, Gram-negative bacteria, fungi and aquatic pathogenic bacteria. The MICs of Cm-CATH2 against most tested strains were within 1.17–18.75μg/ml, especially for Shigella dysentery with MIC value of 1.17μg/ml. Cm-CATH2 at the concentration of 5×MIC required less than 30 min to kill all the tested microbes (E. faecium, E. coli, S. aureus, C. albicans and A. veronii). Especially for E. faecium, Cm-CATH2 showed strong lethal effect within 10 min at 5×MIC and 20 min at 1×MIC. However, the positive control meropenem at 5×MIC required at least 2 h to completely exterminate the E. faecium

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

• Qiao X, Yang H, Gao J, et al. Diversity, immunoregulatory action and structure-activity relationship of green sea turtle cathelicidins. Dev Comp 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.