| Summary: | Antimicrobial peptides (AMPs) are considered as a promising agent to overcome the drug-resistance of bacteria. Large numbers of AMPs have been identified from the skin secretion of <i>Rana pipiens</i>, including brevinins, ranatuerins, temporins and esculentins. In this study, the cDNA precursor of a broad-spectrum antimicrobial peptide, ranatuerin-2Pb, was cloned and identified. Additionally, two truncated analogues, RPa and RPb, were synthesised to investigate the structure-activity relationship of ranatuerin-2Pb. RPa lost antimicrobial activity against <i>Candida albicans</i>, MRSA, <i>Enterococcus faecalis</i> and <i>Pseudomonas aeruginosa</i>, while RPb retained its broad-spectrum antimicrobial activity. Additionally, ranatuerin-2Pb, RPa and RPb demonstrated inhibition and eradication effects against <i>Staphylococcus aureus</i> biofilm. RPb showed a rapid bacterial killing manner via membrane permeabilization without damaging the cell membrane of erythrocytes. Moreover, RPb decreased the mortality of <i>S. aureus</i> infected <i>Galleria mellonella</i> larvae. Collectively, our results suggested that RPb may pave a novel way for natural antimicrobial drug design.
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