OH-CATH peptide

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.