purification and characterization of an antibacterial, antifungal and non hemolytic peptide from rana ridibunda

amphibians have a large variety of antimicrobial peptides that serve as natural innate barriers limiting microbial infection or, in some instances, act as an integral component in response to inflammation or microbial infection. a novel peptide with antibacterial effects and without hemolytic activity was purified from skin secretions of rana ridibunda by multisteps cation-exchange fplc, reversed-phase hplc and was called ridibundin 1. circular dichroism spectra revealed that this peptide strongly prefers to form an amphipathic ?-helical structure in the presence of 50% trifluoroethanol. acting as wide-spectrum microbicides against a variety of bacteria, ridibundin 1 also shows no hemolytic activity on erythrocyte. these properties reveal its unique characteristics and potential therapeutic application