moronecidin-like peptide

**Moronecidin-like peptide** is a synthetic or naturally derived antimicrobial peptide belonging to the piscidin family, characterized by amphipathic α-helical structure and cationic properties[1][4]. It is found in various fish species, including Antarctic fishes (Notothenia coriiceps, Parachaenichthys charcoti) and is similar to moronecidin originally identified from the hybrid striped bass[2][4]. The peptide exhibits potent broad-spectrum **antibacterial** activity against both Gram-positive and Gram-negative bacteria as well as antifungal activity against *Candida albicans*, *Candida glabrata*, and *Candida tropicalis*[1][4]. The mechanism of action involves disruption of microbial cell membranes, leading to cell lysis, which is typical of antimicrobial peptides (AMPs)[1][4]. Its cytotoxicity and hemolytic activity on human cells are minimal, suggesting potential for therapeutic application against fungal infections, especially those caused by *Candida*[1][4]. Modification by C-terminal amidation increases the peptide's activity and can also increase toxicity; the non-amidated form generally exhibits lower cytotoxicity[1][2][4].

Other names

moronecidin-like antimicrobial peptidepiscidin-like peptide