Identification and Characterization of Three New Antimicrobial Peptides from the Marine Mollusk Nerita versicolor (Gmelin, 1791)

Abstract

Mollusks have been widely investigated for antimicrobial peptides because their humoral defense against pathogens is mainly based on these 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 with nanoLC-ESI-MS-MS technology, and three potential antimicrobial peptides (Nv-p1, Nv-p2 and Nv-p3) were identified with bioinformatical predictions and selected for chemical synthesis and evaluation of their biological activity. Database searches showed that two of them show 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 starting at 1.5 µg/mL in the 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.

Antifungal Efficacy of Antimicrobial Peptide Octominin II against Candida albicans

“…Peptides from various sources have shown anticandidal activity against C. albicans. For example, human-based peptides (LL-37, histatin 5, and lactoferrin) [ 26 ], plant-based peptides such as NaD1 from Nicotiana alata [ 27 ], Psd1 from Pisum sativum [ 28 ], marine mollusk-based peptides; Nv-p1, Nv-p2, and Nv-p3 from Nerita versicolor [ 29 ], and the insect peptide Gomesin, Acanthoscurria gomesiana [ 30 ], have been identified and characterized.…”

Applications of tandem mass spectrometry (MS/MS) in antimicrobial peptides field: Current state and new applications

“…This method is commonly used for de novo sequencing of peptides to elucidate the structure of AMPs. Rodriguez, A et al (2023) [ 185 ] performed peptide sequencing analysis with NanoLC-ESI−MS/MS for peptides from the marine shellfish. Punginelli, D et al (2023) [ 186 ] demonstrated that nine new peptides were further identified through high-resolution MS analysis and database searches.…”

The Designed Pore-Forming Antimicrobial Peptide C14R Combines Excellent Activity against the Major Opportunistic Human Pathogen Pseudomonas aeruginosa with Low Cytotoxicity

“…More than 3100 AMPs with certain therapeutic potential have been reported in recent decades [ 6 ], which is of particular interest in the steadily progressing age of resistance development [ 7 ]. They can be isolated from different organismic resources, with mollusks representing a prominent phylum in which interesting molecules have been identified and further developed [ 8 , 9 , 10 , 11 , 12 , 13 , 14 ]. Classical AMPs are characterized by a simple physicochemical mode-of-action due to the way that they can assemble into pores of the target biomembrane via interactions through the peptide residue sidechains [ 15 , 16 ].…”