The native peptide is a cationic amphipathic alpha-helical antimicrobial peptide with potent activity against both Gram-positive and Gram-negative bacteria (PubMed:12709067, PubMed:15222751). It has weak activity against fungi and shows low hemolytic activity (PubMed:12709067, PubMed:15222751). Acts in a synergistic effect in combination with Phylloseptin-B1 or Dermaseptin-B2 at doses that are not active alone (PubMed:12709067, PubMed:15222751). In membrane-mimetic environment, it adopts well-defined helices that lie parallel to the micelle surface (Probable). A short amidated analog (AA 45-67), shows potent activity against Gram-positive, Gram-negative bacteria, and fungi (Probable) (PubMed:15222751, PubMed:17128968). In synergy with Phylloseptin-B1, this analog acts more potently (PubMed:15222751). Its rapid rate for killing E.coli suggests that the membrane is its primary target (PubMed:15222751). This analog is cytotoxic toward differentiated eukaryotic cells (nucleus fragmentation and apoptotic bodies are observed in Hela cells) (PubMed:17128968). This analog has a moderate hemolytic activity (PubMed:17128968). It may interact with anionic phospholipids (DMPG) by decreasing the associated water content of the phospholipid heads (CO), replacing water molecules by peptides themselves (Probable). This analog may have a strong capacity to cross membranes (Probable). Monomer. Highly expressed by the skin glands, and intestine and weakly expressed in brain. Plasticins have huge conformational plasticity. They can display random coil, alpha-helical, beta-sheet or beta-harpin structures. Belongs to the frog skin active peptide (FSAP) family. Plasticin subfamily. Functional studies have principally been done on a short synthetic amidated peptide (AA 45-67) instead of the native peptide (AA 45-70) which is not amidated.