Identification and characterization of three novel antimicrobial peptides from the marine mollusk Nerita versicolor (Gmelin, 1791).

Mollusks have been widely investigated for antimicrobial peptides, because their humoral defense against pathogens is mainly based on such small biomolecules. In this report, we describe the identification of three novel antimicrobial peptides from the marine mollusk Nerita versicolor. A pool of N. versicolor peptides was analyzed by nanoLC-ESI-MS-MS technology and three potential antimicrobial peptides (Nv-p1, Nv-p2 and Nv-p3) were identified by bioinformatical predictions and selected for chemical synthesis and evaluation of their biological activity. Database searches showed that two of them shows partial identity to Histone H4 peptide fragments from other invertebrate species. Structural predictions revealed that they all adopt a random coil structure even when placed near a lipid bilayer patch. Nv-p1, Nv-p2 and Nv-p3 exhibited activity against Pseudomonas aeruginosa. The most active peptide was Nv-p3 with an inhibitory activity of starting at 1.5 µg/mL in radial diffusion assays. The peptides were ineffective against Klebsiella pneumoniae, Listeria monocytogenes, and Mycobacterium tuberculosis. On the other hand, these peptides demonstrated effective antibiofilm action against Candida albicans, Candida parapsilosis and Candida auris, but not against the planktonic cells. None of the peptides had significant toxicity on primary human macrophages and fetal lung fibroblasts at effective antimicrobial concentrations. Our results indicate that N. versicolor-derived peptides represent new AMP sequences and have the potential to be optimized and developed into antibiotic alternatives against bacterial and fungal infections.