Marine Linear Peptides: Isolation, Structure, Biological Properties, Synthesis, Biosynthesis, and Current Advances in Therapeutics

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (30 April 2023) | Viewed by 9081

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Molécules de Communication et Adaptation des Microorganismes, UMR 7245 CNRS, Muséum National d’Histoire Naturelle, 57 rue Cuvier (CP54), 75005 Paris, France
Interests: marine natural product chemistry; marine sponges; marine microbiology; marine chemical ecology; bioactivity; antifouling, anti-biofilm compounds
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Special Issue Information

Dear Colleagues,

The extraordinary biodiversity of the marine world has already offered thousands of varied compounds, such as steroids and terpenoids, alkaloids, polyketides, peptides, etc. The latter represent a large family of marine compounds with a broad spectrum of properties ranging from anticancer to antimicrobial, antioxidant, and anti-inflammatory activities. Marine linear peptides have been particularly successful, leading to two marketed drugs, ziconotide (Prialt®) and Brentuximab vedotin (Adcetris®).

Ziconotide, also known as ω-conotoxin MVIIA, is a 25 amino acid peptide with three disulfide linkages that was clinically approved by the US Food and Drug Administration (FDA) in December 2004 for the intrathecal treatment of severe chronic pain. Ziconotide was shown to block the entry of calcium into neuronal N-type voltage-sensitive calcium channels.

Brentuximab vedotin, a peptide-derived from dolastatin-10 analogue (monomethyl auristatin E), belongs to the very exciting anticancer class of antibody–drug conjugates (ADCs).  Brentuximab vedotin is used for the treatment of relapsed or refractory CD30-positive Hodgkin's lymphoma. So far, five other ADCs have been marketed and 16 ADCs are in clinical trials, at various stages of development. They represent an extremely promising avenue for new molecules with potential anticancer activities.

More recently, gallinamide A, an unusual linear peptide isolated from marine cyanobacteria, known as a potent and selective inhibitor of human cathepsin L, revealed anti-SRAS-CoV2 activity with EC50 values in the nanomolar range.

These successful and growing promises of linear peptides in human therapies have led us to propose a Special Issue entitled “Marine Linear Peptides” to showcase the remarkable family of linear peptides from marine macroorganisms and microorganisms such as cyanobacteria and actinomycetes, including the innovative methodologies used for their identifications, as well as their biological properties and synthesis or biosynthesis. Their potential applications as pharmaceuticals or nutraceuticals will be developed. The progression of some peptide-derived products to clinical trial development should provide to the marine scientist community exciting recent information regarding these attractive families of natural products.

Dr. Marie-Lise Bourguet-Kondracki
Guest Editor

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Keywords

  • Marine linear peptides
  • Conotoxin
  • Marine cyanobacteria
  • Marine actinomycetes
  • Biological activity
  • Pharmaceuticals
  • Nutraceuticals
  • Marine natural products

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Published Papers (2 papers)

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Research

25 pages, 7801 KiB  
Article
Bioactive Peptides from Skipjack Tuna Cardiac Arterial Bulbs: Preparation, Identification, Antioxidant Activity, and Stability against Thermal, pH, and Simulated Gastrointestinal Digestion Treatments
by Wei-Wei Cai, Xiao-Meng Hu, Yu-Mei Wang, Chang-Feng Chi and Bin Wang
Mar. Drugs 2022, 20(10), 626; https://doi.org/10.3390/md20100626 - 30 Sep 2022
Cited by 90 | Viewed by 6858
Abstract
Cardiac arterial bulbs of Skipjack tuna (Katsuwonus pelamis) are rich in elastin, and its hydrolysates are high quality raw materials for daily cosmetics. In order to effectively utilizing Skipjack tuna processing byproducts-cardiac arterial bulbs and to prepare peptides with high antioxidant [...] Read more.
Cardiac arterial bulbs of Skipjack tuna (Katsuwonus pelamis) are rich in elastin, and its hydrolysates are high quality raw materials for daily cosmetics. In order to effectively utilizing Skipjack tuna processing byproducts-cardiac arterial bulbs and to prepare peptides with high antioxidant activity, pepsin was selected from six proteases for hydrolyzing proteins, and the best hydrolysis conditions of pepsin were optimized. Using ultrafiltration and chromatographic methods, eleven antioxidant peptides were purified from protein hydrolysate of tuna cardiac arterial bulbs. Four tripeptides (QGD, PKK, GPQ and GLN) were identified as well as seven pentapeptides (GEQSN, GEEGD, YEGGD, GEGER, GEGQR, GPGLM and GDRGD). Three out of them, namely the tripeptide PKK and the pentapeptides YEGGD and GPGLM exhibited the highest radical scavenging activities on 2,2-diphenyl-1-picrylhydrazyl (DPPH), hydroxyl, 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) and superoxide anion assays. They also showed to protect plasmid DNA and HepG2 cells against H2O2-induced oxidative stress. Furthermore, they exhibited high stability under temperature ranged from 20-100 °C, pH values ranged from 3-11, and they simulated gastrointestinal digestion for 240 min. These results suggest that the prepared eleven antioxidant peptides from cardiac arterial bulbs, especially the three peptides PKK, YEGGD, and GPGLM, could serve as promising candidates in health-promoting products due to their high antioxidant activity and their stability. Full article
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21 pages, 6912 KiB  
Article
Genome-Wide Identification, Evolutionary Analysis, and Expression Patterns of Cathepsin Superfamily in Black Rockfish (Sebastes schlegelii) following Aeromonas salmonicida Infection
by Yuqing Li, Xingchun Li, Pei Zhang, Defeng Chen, Xinran Tao, Min Cao, Chao Li and Qiang Fu
Mar. Drugs 2022, 20(8), 504; https://doi.org/10.3390/md20080504 - 3 Aug 2022
Cited by 2 | Viewed by 2335
Abstract
Cathepsins are lysosomal cysteine proteases belonging to the papain family and play crucial roles in intracellular protein degradation/turnover, hormone maturation, antigen processing, and immune responses. In the present study, 18 cathepsins were systematically identified from the fish S. schlegelii genome. Phylogenetic analysis indicated [...] Read more.
Cathepsins are lysosomal cysteine proteases belonging to the papain family and play crucial roles in intracellular protein degradation/turnover, hormone maturation, antigen processing, and immune responses. In the present study, 18 cathepsins were systematically identified from the fish S. schlegelii genome. Phylogenetic analysis indicated that cathepsin superfamilies are categorized into eleven major clusters. Synteny and genome organization analysis revealed that whole-genome duplication led to the expansion of S. schlegelii cathepsins. Evolutionary rate analyses indicated that the lowest Ka/Ks ratios were observed in CTSBa (0.13) and CTSBb (0.14), and the highest Ka/Ks ratios were observed in CTSZa (1.97) and CTSZb (1.75). In addition, cathepsins were ubiquitously expressed in all examined tissues, with high expression levels observed in the gill, intestine, head kidney, and spleen. Additionally, most cathepsins were differentially expressed in the head kidney, gill, spleen, and liver following Aeromonas salmonicida infection, and their expression signatures showed tissue-specific and time-dependent patterns. Finally, protein–protein interaction network (PPI) analyses revealed that cathepsins are closely related to a few immune-related genes, such as interleukins, chemokines, and TLR genes. These results are expected to be valuable for comparative immunological studies and provide insights for further functional characterization of cathepsins in fish species. Full article
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