Development of a novel anti-biofilm peptide derived from profilin ofSpodoptera frugiperda

Abstract

Candidayeast infections are the fourth leading cause of death worldwide. Peptides with antimicrobial activity are a promising alternative treatment for such infections. Here, the antifungal activity of a new antimicrobial peptide-PEP-IA18-was evaluated againstCandidaspecies. PEP-IA18 was designed from the primary sequence of profilin, a protein fromSpodoptera frugiperda,and displayed potent activity againstCandida albicansandCandida tropicalis, showing a minimum inhibitory concentration (MIC) of 2.5 mu M. Furthermore, the mechanism of action of PEP-IA18 involved interaction with the cell membrane (ergosterol complexation). Treatment at MIC and/or 10 x MIC significantly reduced biofilm formation and viability. PEP-IA18 showed low toxicity toward human fibroblasts and only revealed hemolytic activity at high concentrations. Thus, PEP-IA18 exhibited antifungal and anti-biofilm properties with potential applicability in the treatment of infections caused byCandidaspecies.