A Deep Dive into the Ocean: Evaluation of Marine Compounds Bioactivity in the Omics Era

A special issue of Marine Drugs (ISSN 1660-3397). This special issue belongs to the section "Marine Biotechnology Related to Drug Discovery or Production".

Deadline for manuscript submissions: 30 September 2024 | Viewed by 4144

Special Issue Editors


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Guest Editor
Department of Pharmacy, University of Naples Federico II, Via Tommaso De Amicis 95, 80131 Naples, Italy
Interests: functional proteomics; global proteomics; drug-target deconvolution; mass spectrometry; biochemistry; metabolomics; metabolites quantification
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Guest Editor
Department of Pharmacy, University of Naples 'Federico II', Via Tommaso De Amicis 95, 80131 Naples, Italy
Interests: proteomics; functional proteomics; metabolomics; analytical chemistry; small-molecules/proteins interactions; marine-inspired compounds
Special Issues, Collections and Topics in MDPI journals

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Guest Editor
Department of Pharmacy, University of Salerno, Via Giovanni Paolo II 132, 84084 Fisciano, SA, Italy
Interests: skin wound healing; angiogenesis; endothelial to mesenchymal and epithelial to mesenchymal transition; cancer biology; cell transfection; in vitro cultures; wound healing in mice; cell migration and invasion; pharmacology in general; extracellular vesicles isolation, characterization and use
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Comprising approximately half of the world's biodiversity, the marine environment represents a massive source of structurally multifaceted compounds, showing a range of complex and biologically relevant chemotypes. Indeed, marine products have been, and still are, a valuable source of drug discovery, being endowed with a wide spectrum of bioactivity. Despite the recent advances, a plethora of marine bioactive compounds still need to be explored to elucidate their mechanism of action. In this scenario, omics sciences represent a robust toolbox of complementary approaches, which clarify several aspects of bioactive molecule behavior, from its ability to influence certain cell transcriptomes, proteomes and/or metabolomes regarding their ability to specifically bind a set of proteins and thus exert their biological functions.

This Special Issue aims to showcase original research or review papers exploring marine bioactive compounds using omics strategies coupled with molecular biology and/or pharmacological approaches to obtain an in-depth characterization of their mechanisms of action.

Dr. Elva Morretta
Dr. Maria Chiara Monti
Dr. Raffaella Belvedere
Guest Editors

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Marine Drugs is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • functional proteomics
  • proteins expression profiling
  • proteins post-translational modifications analysis
  • metabolomics
  • transcriptomics
  • multi-omics approaches
  • biological activity
  • pharmacological profiling.

Published Papers (3 papers)

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Research

12 pages, 3461 KiB  
Article
Synthetic ShK-like Peptide from the Jellyfish Nemopilema nomurai Has Human Voltage-Gated Potassium-Channel-Blocking Activity
by Ye-Ji Kim, Yejin Jo, Seung Eun Lee, Jungeun Kim, Jae-Pil Choi, Nayoung Lee, Hyokyoung Won, Dong Ho Woo and Seungshic Yum
Mar. Drugs 2024, 22(5), 217; https://doi.org/10.3390/md22050217 - 13 May 2024
Viewed by 435
Abstract
We identified a new human voltage-gated potassium channel blocker, NnK-1, in the jellyfish Nemopilema nomurai based on its genomic information. The gene sequence encoding NnK-1 contains 5408 base pairs, with five introns and six exons. The coding sequence of the NnK-1 precursor is [...] Read more.
We identified a new human voltage-gated potassium channel blocker, NnK-1, in the jellyfish Nemopilema nomurai based on its genomic information. The gene sequence encoding NnK-1 contains 5408 base pairs, with five introns and six exons. The coding sequence of the NnK-1 precursor is 894 nucleotides long and encodes 297 amino acids containing five presumptive ShK-like peptides. An electrophysiological assay demonstrated that the fifth peptide, NnK-1, which was chemically synthesized, is an effective blocker of hKv1.3, hKv1.4, and hKv1.5. Multiple-sequence alignment with cnidarian Shk-like peptides, which have Kv1.3-blocking activity, revealed that three residues (3Asp, 25Lys, and 34Thr) of NnK-1, together with six cysteine residues, were conserved. Therefore, we hypothesized that these three residues are crucial for the binding of the toxin to voltage-gated potassium channels. This notion was confirmed by an electrophysiological assay with a synthetic peptide (NnK-1 mu) where these three peptides were substituted with 3Glu, 25Arg, and 34Met. In conclusion, we successfully identified and characterized a new voltage-gated potassium channel blocker in jellyfish that interacts with three different voltage-gated potassium channels. A peptide that interacts with multiple voltage-gated potassium channels has many therapeutic applications in various physiological and pathophysiological contexts. Full article
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17 pages, 2081 KiB  
Article
Identification of Mortalin as the Main Interactor of Mycalin A, a Poly-Brominated C-15 Acetogenin Sponge Metabolite, by MS-Based Proteomics
by Elva Morretta, Alessandra Capuano, Gilda D’Urso, Antonia Voli, Matteo Mozzicafreddo, Sonia Di Gaetano, Domenica Capasso, Marina Sala, Maria Carmina Scala, Pietro Campiglia, Vincenzo Piccialli and Agostino Casapullo
Mar. Drugs 2024, 22(2), 52; https://doi.org/10.3390/md22020052 - 23 Jan 2024
Viewed by 1448
Abstract
Mycalin A (MA) is a polybrominated C-15 acetogenin isolated from the marine sponge Mycale rotalis. Since this substance displays a strong antiproliferative bioactivity towards some tumour cells, we have now directed our studies towards the elucidation of the MA interactome through functional [...] Read more.
Mycalin A (MA) is a polybrominated C-15 acetogenin isolated from the marine sponge Mycale rotalis. Since this substance displays a strong antiproliferative bioactivity towards some tumour cells, we have now directed our studies towards the elucidation of the MA interactome through functional proteomic approaches, (DARTS and t-LIP-MS). DARTS experiments were performed on Hela cell lysates with the purpose of identifying MA main target protein(s); t-LiP-MS was then applied for an in-depth investigation of the MA–target protein interaction. Both these techniques exploit limited proteolysis coupled with MS analysis. To corroborate LiP data, molecular docking studies were performed on the complexes. Finally, biological and SPR analysis were conducted to explore the effect of the binding. Mortalin (GRP75) was identified as the MA’s main interactor. This protein belongs to the Hsp70 family and has garnered significant attention due to its involvement in certain forms of cancer. Specifically, its overexpression in cancer cells appears to hinder the pro-apoptotic function of p53, one of its client proteins, because it becomes sequestered in the cytoplasm. Our research, therefore, has been focused on the possibility that MA might prevent this sequestration, promoting the re-localization of p53 to the nucleus and facilitating the apoptosis of tumor cells. Full article
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15 pages, 4855 KiB  
Article
Taxonomic, Phylogenomic and Bioactivity Profiling of Novel Phycosphere Bacterium from Model Cyanobacterium Synechococcus elongatus PCC 7942
by Xiaoling Zhang, Jiaquan Xu, Jun Dai, Lei Zhang, Lijuan Feng, Xiaoqing Tian and Qiao Yang
Mar. Drugs 2024, 22(1), 36; https://doi.org/10.3390/md22010036 - 7 Jan 2024
Viewed by 1833
Abstract
Phycosphere niches host rich microbial consortia that harbor dynamic algae–bacteria interactions with fundamental significance in varied natural ecosystems. Hence, culturing the uncultured microbial majority of the phycosphere microbiota is vital for deep understanding of the intricate mechanisms governing the dynamic interactions, and also [...] Read more.
Phycosphere niches host rich microbial consortia that harbor dynamic algae–bacteria interactions with fundamental significance in varied natural ecosystems. Hence, culturing the uncultured microbial majority of the phycosphere microbiota is vital for deep understanding of the intricate mechanisms governing the dynamic interactions, and also to provide novel and rich microbial resources, and to discover new natural bioactive metabolites. Synechococcus elongatus PCC 7942 is a robust model cyanobacterium widely used in environment, synthesis biology, and biotechnology research. To expand the number of novel phycosphere species that were brought into culture and to discover the natural bioactivities, we presented a new yellow-pigmented bacterium named ABI-127-1, which was recovered from the phycosphere of PCC 7942, using an optimized bacterial isolation procedure. Combined polyphasic taxonomic and phylogenomic characterization was performed to confidently identify the new isolate as a potential novel species belonging to the genus Qipengyuania. The observed bioactivity of strain ABI-127-1 with promoting potential towards the growth and CO2 fixation efficiency of the host microalgae was measured. Additionally, the bacterial production of active bioflocculant exopolysaccharides was evaluated after culture optimization. Thus, these findings revealed the potential environmental and biotechnological implications of this new microalgae growth-promoting bacterium isolated from the phycosphere microenvironment. Full article
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