Insights into the antifungal properties and modes of action of a recombinant hepcidin, rAd-Hep from the shrimp scad, Alepes djedaba (Forsskål, 1775).

Antimicrobial peptides are short, mostly cationic and amphipathic molecules crucial for host defence. Among these, hepcidins are a family of cysteine rich peptides, with HAMP1 hepcidins playing a dual role in iron metabolism and antimicrobial defense. Recently, recombinantly produced Alepes djedaba hepcidin, rAd-Hep was characterized and its antibacterial potential against various pathogens have been discerned. Herein, we investigated the antifungal nature and modes of action of rAd-Hep against some fungal pathogens. The peptide was found to be active against both filamentous fungi and yeasts viz., Aspergillus flavus, Aspergillus sydowii, Fusarium solani, Penicillium citrinum, Candida albicans and Saccharomyces cerevisiae. The peptide acted via membrane permeabilization creating pores of ∼0.7-1.4 nm radii, ROS generation, chromatin condensation and DNA binding. The recombinant hepcidin, rAd-Hep can be considered as a promising candidate for future endeavors in antifungal therapies.