Atypical cationic antimicrobial peptide with potent activity against Gram-negative and Gram-positive bacteria (PubMed:16401077, PubMed:18637027). Acts by inducing permeabilization of bacterial membrane (PubMed:16401077). In vitro, also shows chemoattractant activity, which is mediated through a G protein-coupled receptor (probably FPR2 coupled to the ERK1/2 MAPK kinase pathway) (PubMed:18637027). Has slow-kinetic self-association and amyloid-like properties that modulate its activity (PubMed:18637027, PubMed:24146759). The soluble, weakly self-associated forms act on leukocytes to promote chemotaxis but have low antibacterial activity, the oligomers exhibit potent antimicrobial activity, whereas the amyloid-like fibrils have a very weak antibacterial activity (PubMed:18637027). The membrane composition has a great influence on the peptide behavior (PubMed:24146759). The peptide induces membrane leakage and insertion to a lesser extent in model membranes of the anionic lipid phospatidylglycerol (PG) than in the model membranes of the zwitterionic lipid phosphatidylcholine (PC) vesicles (PubMed:24146759). It forms more fibrils in PC than in PG (PubMed:24146759). Membrane perturbations are more observed in the presence of PG than in the presence of PC (PubMed:24146759). The peptide shows low hemolytic activity (PubMed:16401077). Thermostable. Monomer and/or weakly self-associated, oligomer, and amyloid-like fibril (PubMed:18637027, PubMed:24146759). Can adopt a monomeric nonamphipathic alpha-helical conformation, possibly with the aid of its cationic N- and C-termini, when bound to anionic membranes (Probable) (PubMed:16401077). Forms stable and ordered beta-sheet aggregates in aqueous environment or when bound to anionic or zwitterionic phospholipid vesicles (PubMed:18637027, PubMed:24146759). Expressed by the skin glands. Has a highly hydrophobic core sequence flanked at either side by cationic termini. The mutant DRS S9r3 shows antiviral activity against HIV. Belongs to the frog skin active peptide (FSAP) family.