The antibacterial activity of Temporin A and its analogues against strains used for the evaluation of preservatives

摘要

Peptide antibiotics are secreted by most organisms,protecting them against microbial infection.These peptides provide a major defence mechanism in bacteria,plants and lower animals and the first line of host defence before the mobilization of specific immunity in vertebrates.Actually,antimicrobial peptides can be rapidly activated after invasion of the host by microbial agents,inhibiting parasitic growth immediately after infection.Among these animal-derived antimicrobial agents are the temporins,linear 10-13 residues long peptides with a net positive charge and an amidated C-terminus discovered in the skin of the European red frog Rana temporaria more than 8 years ago.They are among the smallest antimicrobial peptides found in nature.Temporin A is a basic,highly hydrophobic,antimicrobial peptide amide(FLPLIGRVLSG1L-NH_2)that has variable antibiotic activity against a broad-spectrum of microorganisms.Like the other temporins,it is active against clinically important antibiotic-resistant gram-positive cocci.Owing to the low toxicity of endogenous antimicrobial peptides,particularly high hope is attributed to the possibility to use them as biopharmaceuticals in modern chemotherapy of infectious diseases.In the future they can be used for preservation of medicines,cosmetics and food as well.