Temporins
The temporins belong to a family of short (8–17 amino acids), hydrophobic, C-terminally α-amidated peptides with antibacterial and antifungal properties that are synthesized in the skins of a wide range of North American and Eurasian frogs of the Ranidae family. Temporins adopt an α-helical conformation in hydrophobic environments and have the ability to perturb the integrity of target cell membranes. Not all temporins are cationic, but the number of positively charged amino acids correlates with antimicrobial potency. Temporins are mostly effective against Gram-positive bacteria, but some are also active against Gram-negative bacteria. Temporins show potential for development into therapeutically valuable anti-infective agents, particularly for use against antibiotic-resistant Gram-positive bacteria such as methicillin-resistant Staphylococcus aureus (MRSA) and Enterococcus faecalis, against anaerobic pathogens such as Clostridium difficile, and against the protozoan parasite Leishmania spp. Although the clinical usefulness of naturally occurring temporins is limited by high hemolytic activity, noncytotoxic analogs have been designed.
POTENTIAL CLINICAL AND COMMERCIAL APPLICATIONS The emergence of strains of pathogenic microorganisms with resistance to commonly used antibiotics constitutes a serious threat to public health that has necessitated a search for new types of antimicrobial agents. The temporins are promising candidates for development into clinically useful antiinfectives, particularly with regard to topical applications, such as treatment of acne vulgaris and infected foot ulcers in diabetic patients. Several temporins show high potency in vitro against nosocomial Gram-positive pathogens such as MRSA7,13 and antibiotic-resistant strains of E. faecalis.
No comments:
Post a Comment