Non-amphipathic alpha-helical antimicrobial peptide with potent activity against some Gram-positive bacteria (including methicillin-resistant Staphylococcus aureus (MRSA)), weak activity against Gram-negative bacteria and no activity against fungi (PubMed:20308076, PubMed:26181487, PubMed:27915018). Permeabilizates membranes through a detergent-like effect probably via the carpet mechanism (PubMed:20308076). More precisely, it strongly and selectively perturbs anionic bilayers membranes by interacting with the polar headgroups and the glycerol backbone region of the phospholipids, hence disrupting the acyl chain packing of the bilayer (PubMed:20308076). Is not active against Leishmania (promastigote and axenic amastigote forms) (PubMed:20308076). Does not show hemolytic activity (PubMed:20308076, PubMed:26181487). Does not show toxicity for human THP-1-derived macrophages (PubMed:26181487). Inserts into the lipid bilayer with an in-plane (parallel) orientation. Has potential application in preventing biofilm formation on medical devices, since it has the ability to prevent methicillin-resistant S.aureus biofilm formation on the polyethylene terephthalate (PET) surface, which is widely used in making prosthetic heart valves cuffs and other bio devices. Owing to its short length, simple composition, and broad spectrum of antimicrobial activity, this peptide is a promising candidate for the development of a new class of antibiotics (PubMed:20308076). The analog [p-(t)BuF(2), R5]SHf emerged as a highly potent bactericidal ultrashort peptide, but weakly or non-cytotoxic against mammalian cells (PubMed:26181487). Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily.