Amphipathic alpha-helical antimicrobial peptide with potent activity against both Gram-negative and Gram-positive bacteria, and against fungi (PubMed:9022710, PubMed:12133008, PubMed:16867990, PubMed:18370376, PubMed:31358802). Mainly acts by causing perturbation of bilayer integrity of both neutral and negatively charged membranes, probably by forming pore-like openings (PubMed:12133008, PubMed:31358802). Also displays anti-leishmania activity by damaging parasite membrane (By similarity). Shows hemolytic activity (PubMed:12133008). Also shows cytotoxicity against cancer cell lines (PubMed:12133008). Strongly binds to lipopolysaccharides (LPS) and its lipid A portion (PubMed:16801429) (Probable). Improves temporin-A and temporin-B activities by preventing their homo-oligomerization in LPS (PubMed:16867990, PubMed:21586570). In vivo, its simultaneous administration with beta-lactam antibiotics produces the highest antimicrobial activities and the strongest reduction in plasma LPS and TNF-alpha levels, resulting in the highest survival rates in rat models of septic shock (PubMed:16801429). Adopts monomeric helical conformations when bound to bacterial (anionic) and eukaryotic (zwitterionic) model membranes (Probable). May also oligomerize as homo-dimers or -trimers in Gram-negative bacteria mimetic membranes, and from homo-dimers to -pentamers in Gram-positive bacteria mimetic membranes (Probable). Adopts an antiparallel dimeric helical structure when complexed with LPS micelles (PubMed:21586570). This dimeric helical structure may interact with the lipid A domain of LPS (Probable). Contact and insertion into membrane begin at the N-terminus. Expressed by the skin glands. Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily.