OH-CATH peptide

OH-CATH peptide

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

KRFKKFFKKLKNSVKKRAKKFFKKPRVIGVSIPF

Lys-Arg-Phe-Lys-Lys-Phe-Phe-Lys-Lys-Leu-Lys-Asn-Ser-Val-Lys-Lys-Arg-Ala-Lys-Lys-Phe-Phe-Lys-Lys-Pro-Arg-Val-Ile-Gly-Val-Ser-Ile-Pro-Phe

34

97.2%

Synthetic

Powder

Rich in lysines (35%). Active against E. cloacae (MIC 1 ug/ml), E. aerogenes (MIC 4 ug/ml), E. coli (MIC 6-20 ug/ml), S. aureus (MIC 4 ug/ml), and P. aeruginosa PAO1 (MIC 2 ug/ml). Predicted to be helical based on the known structure of human LL-37. OH-CATH30 is obtained by removing the N-terminal 4 residues. OH-CM6 is obtained by further shortening OH-CATH30 by deleting the C-terminal 10 residues followed by mutations. These derivatives are active against indicator and resistant bacterial strains (MIC in the range of 1.5-25 ug/ml). Activity is reduced in the presence of serum. However, the D-form is stable for at least 12 h. These peptides appear to work on membranes as indicated by rapid killing in 60 min (2XMIC) and dye leakage. Both OH-CATH30 and OH-CM6 displayed in vivo efficacy in reducing drug-resistant E. coli burdens in the neutropenic thigh infection animal model:mouse or murine bacteremia model. It also showed protective effects on E. coli induced rabbit urinary tract infection models (animal model:rabbit)( Zhang et al., 2013). The D-form of these peptides is also active in vivo although with higher cytotoxicity ( Li SA et al. 2010). In addition, topical application of OH-CATH30 is efficacious against drug-resistant P. aeruginosa keratitis ( Li SA et al., 2014). Updated 13/4/2012; Feb2013; 3/2014 GW. OH-CATH has Antibacterial activity. OH-CATH was found in king cobra, Ophiophagus hannah.

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

• Zhao H, Gan TX, Liu XD, et al. Identification and characterization of novel reptile cathelicidins from elapid snakes. Peptides. 2008;29(10):1685-91.

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.