| Summary: | Antimicrobial peptides are genetically encoded defense molecules found in all types of organisms that encounter microbes. One class of antimicrobial peptides, Piscidins, are reported to possess significant therapeutic activities. Piscidins from Nile Tilapia (Oreochromis niloticus) include five known members, namely Tilapia piscidin 1 (TP-1), Tilapia piscidin 2 (TP-2), Tilapia piscidin 3 (TP-3), Tilapia piscidin 4 (TP-4) and Tilapia piscidin 5 (TP-5). Among these peptides, TP4 (PDB ID: 5H2S) has become the most promising candidate for commercial application. TP4 is a 25 amino acid polypeptide with prominent alpha-helical secondary structure. Furthermore, it is a cationic, amphipathic peptide that has been reported to exhibit anticancer, antimicrobial, immunomodulatory and wound healing properties. In this manuscript, we review recent work on TP4, describing its potential utility and application in drug discovery.
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