Cm-CATH2 peptide

Cm-CATH2 peptide

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

1 Vial

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

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) is a strong acid, which is commonly used to cleave synthesized peptides from solid-phase resins and is also used to improve HPLC performance in the peptide purification step. By default, custom peptides are delivered as lyophilized TFA salts, and can contain as much as 10-45% TFA.

TFA in custom peptides can cause inexplicable discrepancies in subsequent assay data. For instance, TFA in nM concentrations has been shown to interfere with cellular assays, inhibiting cellular proliferation in some instances, and increasing cell viability in others . It has also been found to be an unintended allosteric modulator of the glycine receptor, GlyR.

TFA Removal Service is recommended for:

• Peptides that will be used in cellular assays
• Peptides that will be used as APIs or in manufactured products
• For hydrophilic peptides containing numerous basic residues