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National Committee on Marine Sciences (NCMS)

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    Synthesis and biological evaluation of cyanobacterial-inspired peptides
    Casanova, Jannelle R.; Villaraza, Aaron Joseph L.; Salvador-Reyes, Lilibeth (Philippine-American Academy of Science and Engineering, 2024-03-18)
    Cyanobacteria are known producers of structurally diverse and potent natural products; the majority are peptides with unique modifications. Yet, there remains a huge underexplored chemodiversity from cyanobacteria. Here, we designed a linear octapeptide as a product of combinatorial peptide design inspired by the natural products from the filamentous cyanobacteria Hapalosiphon welwitschii and Leptolyngbya sp. The target peptide was synthesized via solid-phase peptide synthesis (SPPS) using fluorenylmethyloxycarbonyl-protecting group (Fmoc) strategy. Structural diversity was expanded by the substitution of unnatural amino acids to yield five analogues. The structure and sequence of the synthesized peptides were confirmed using nuclear magnetic resonance (NMR) spectroscopy and mass spectrometry (MS). Biological activity evaluation was done; with none of the peptides showing antimicrobial or cytotoxic activities against microbial pathogens and mammalian cells, respectively. To our knowledge, this study is the first to report a combinatorial peptide design inspired by a natural product and a predicted biosynthetic product. This strategy of peptide design expands the chemistry of a known bioactive natural product with the aid of unexplored cyanobacterial biosynthetic gene clusters.
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    Diversity and novelty of venom peptides from Conus (Asprella) rolani revealed by analysis of its venom duct transcriptome
    Taguchi, Ryoichi; Masacupan, Dan Jethro; Lluisma, Arturo (Philippine-American Academy of Science and Engineering, 2024-04-22)
    Conus species in the sub-genus Asprella are poorly studied because they inhabit deep-water habitats. To date, only a few peptides have been characterized from this clade. In this study, the venom duct transcriptome of a member of this clade, Conus rolani, was mined for potential conopeptides. Using a highthroughput RNA sequencing platform (Illumina) and a multiple k-mer de novo assembly, we found 103 putative conopeptide precursor amino acid sequences, including the few peptides previously reported for this species. The sequences, predominantly novel based on amino acid sequence, were diverse, comprising 36 gene superfamilies (including the “unassigned” superfamilies). As observed in other Conus species, the O1 gene superfamily was the most diverse (12 distinct sequences) but interestingly none of the sequences were found to contain the conserved amino acids associated with certain bioactivities in peptides found in piscivorous Conus species. The O2 superfamily was also highly diverse but conikot-ikot and an unassigned superfamily (MMSRMG) were more diverse than the rest of the superfamilies. In terms of gene expression levels, the understudied MEFRR paralog of the ancestral divergent M---L-LTVA superfamily was found to be the most highly expressed in the transcriptome, suggesting a novel role. Additionally, a conopeptide with high sequence similarity to A2 secretory group XII phospholipases is the first reported member of this phospholipase group in Conus and potentially represents a novel superfamily, expanding the catalog of known phospholipases present in cone snail venoms. The discovery of these putative conopeptides provides the first but early glimpse of the diversity and novelty of the peptides in the Asprella group and sets the stage for their functional characterization.
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    Total synthesis and bioactivity evaluation of hydrophobic microcionamide‐inspired peptides
    Inocentes, Carl Rogel V.; Salvador‐Reyes, Lilibeth A.; Villaraza, Aaron Joseph L. (Wiley, 2023-01)
    In this report, we describe the facile synthesis of four microcionamide-inspired peptides where the atypical 2-phenylethylenamine (2-PEA) functional group in the marine natural product, microcionamide A, was replaced with a similarly-aromatic but more easily incorporated tryptophan (Trp) residue. Compounds 1–4 were synthesized using a standard Fmoc-based solid-phase synthesis strategy followed by iodine-mediated on-resin cyclization for disulfide-bridged compounds 1–3. Compound 1 showed antimicrobial activity against Staphylococcus aureus and Pseudomonas aeruginosa, with minimum inhibitory concentrations (MICs) of 9.1 μM and 15 μM, respectively. The inactivity of alanine analogs 2–4 against these pathogens suggests that the N-terminal Val, the cyclic scaffold, the contiguous Ile residues, and consequently, the hydrophobicity of compound 1 are essential for antibacterial activity. Compound 1 also favorably exhibited minimal cytotoxicity against normal mammalian cell lines. In summary, we have synthesized an analog of microcionamide A where replacement of the 2-PEA moiety with a Trp residue retained the antibacterial activity and with favorably low cytotoxicity.