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Marine Drugs
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Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential IV
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Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential IV

A special issue of Marine Drugs (ISSN 1660-3397). This special issue belongs to the section "Structural Studies on Marine Natural Products".

Deadline for manuscript submissions: closed (31 August 2023) | Viewed by 15612

Special Issue Editor

Prof. Dr. Tatiana V. Ovchinnikova

E-Mail Website
Guest Editor
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
Interests: marine natural products; marine peptides; innate immunity; host defense peptides; molecular mechanisms of antimicrobial and anticancer activity; structure elucidation; structure-function relationship; bioengineering; drug design; peptide antibiotics; peptide anticancer agents; drug resistance; bioorganic chemistry; biotechnology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Marine peptides that are diverse in structure and function have been found in various phyla, and their number has dynamically grown in recent years. Some of them are evolutionary ancient molecular factors of innate immunity that play a key role in host defense. A plethora of biological activities, including antibacterial, antifungal, antiviral, cytotoxic, neurotoxic, anticoagulant, antifreeze, endotoxin-binding, and immune-modulating activities, make marine peptides an attractive molecular basis for the design of innovative antibiotics, anticancer drugs, analgesics, medicines for neurological disorders, etc.

The fourth edition of the Special Issue “Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential IV” aims to collect papers on up-to-date information regarding the isolation, structural elucidation, functional characterization, and therapeutic potential evaluation of peptides isolated from marine organisms. The chemical synthesis and biotechnological production of marine peptides and their mimetics will also be a focus in this Special Issue. In addition, this Special Issue will publish new results deriving from peptidomic and bioinformatic approaches for the development of new drugs.

Prof. Dr. Tatiana V. Ovchinnikova
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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

  • marine peptides
  • structure
  • function
  • chemical synthesis
  • biotechnological production
  • peptidomics
  • therapeutic potential
  • antibacterial
  • antifungal
  • antiviral
  • cytotoxic
  • neurotoxic
  • anticancer
  • anticoagulant
  • endotoxin-binding
  • host defense
  • innate immunity
  • toxins
  • peptide drugs

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Related Special Issues

Published Papers (6 papers)

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Research

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18 pages, 25300 KiB  
Article
Alcalase-Assisted Mytilus edulis Hydrolysate: A Nutritional Approach for Recovery from Muscle Atrophy
by R. P. G. S. K. Amarasiri, Jimin Hyun, Sang-Woon Lee, Jin Kim, You-Jin Jeon and Jung-Suck Lee
Mar. Drugs 2023, 21(12), 623; https://doi.org/10.3390/md21120623 - 29 Nov 2023
Cited by 2 | Viewed by 2137
Abstract
Muscle atrophy is a complex physiological condition caused by a variety of reasons, including muscle disuse, aging, malnutrition, chronic diseases, immobilization, and hormonal imbalance. Beyond its effect on physical appearance, this condition significantly reduces the quality of human life, thus warranting the development [...] Read more.
Muscle atrophy is a complex physiological condition caused by a variety of reasons, including muscle disuse, aging, malnutrition, chronic diseases, immobilization, and hormonal imbalance. Beyond its effect on physical appearance, this condition significantly reduces the quality of human life, thus warranting the development of preventive strategies. Although exercising is effective in managing this condition, it is applicable only for individuals who can engage in physical activities and are not bedridden. A combination of exercise and nutritional supplementation has emerged as a more advantageous approach. Here, we evaluated the effects of enzyme-assisted hydrolysates of Mytilus edulis prepared using Protamex (PMH), Alcalase (AMH), or Flavourzyme (FMH) in protecting against muscle atrophy in a dexamethasone (Dex)-induced muscular atrophy model in vitro and in vitro. Alcalase-assisted M. edulis hydrolysate (AMH) was the most efficient among the tested treatments and resulted in higher protein recovery (57.06 ± 0.42%) and abundant amino acid composition (43,158 mg/100 g; 43.16%). AMH treatment also escalated the proliferation of C2C12 cells while increasing the total number of nuclei, myotube coverage, and myotube diameter. These results were corroborated by a successful reduction in the levels of proteins responsible for muscle atrophy, including E3 ubiquitin ligases, and an increase in the expression of proteins associated with muscle hypertrophy, including myogenin and MyHC. These results were further solidified by the successful enhancement of locomotor ability and body weight in zebrafish following AMH treatment. Thus, these findings highlight the potential of AMH in recovery from muscle atrophy. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential IV)
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14 pages, 2465 KiB  
Article
Affinity Purification and Molecular Characterization of Angiotensin-Converting Enzyme (ACE)-Inhibitory Peptides from Takifugu flavidus
by Yongchang Su, Shicheng Chen, Shuji Liu, Yin Wang, Xiaoting Chen, Min Xu, Shuilin Cai, Nan Pan, Kun Qiao, Bei Chen, Suping Yang and Zhiyu Liu
Mar. Drugs 2023, 21(10), 522; https://doi.org/10.3390/md21100522 - 29 Sep 2023
Cited by 2 | Viewed by 2099
Abstract
An affinity chromatography filler of CNBr-activated Sepharose 4B-immobilized ACE was used to purify ACE-inhibitory peptides from Takifugu flavidus protein hydrolysate (<1 kDa). Twenty-four peptides with an average local confidence score (ALC) ≥ 80% from bounded components (eluted by 1 M NaCl) were identified [...] Read more.
An affinity chromatography filler of CNBr-activated Sepharose 4B-immobilized ACE was used to purify ACE-inhibitory peptides from Takifugu flavidus protein hydrolysate (<1 kDa). Twenty-four peptides with an average local confidence score (ALC) ≥ 80% from bounded components (eluted by 1 M NaCl) were identified by LC-MS/MS. Among them, a novel peptide, TLRFALHGME, with ACE-inhibitory activity (IC50 = 93.5 µmol·L−1) was selected. Molecular docking revealed that TLRFALHGME may interact with the active site of ACE through H-bond, hydrophobic, and electrostatic interactions. The total binding energy (ΔGbinding) of TLRFALHGME was estimated to be −82.7382 kJ·mol−1 by MD simulations, indicating the favorable binding of peptides with ACE. Furthermore, the binding affinity of TLRFALHGME to ACE was determined by surface plasmon resonance (SPR) with a Kd of 80.9 µmol, indicating that there was a direct molecular interaction between them. TLRFALHGME has great potential for the treatment of hypertension. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential IV)
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17 pages, 3546 KiB  
Article
Antioxidant, Collagenase Inhibitory, and Antibacterial Effects of Bioactive Peptides Derived from Enzymatic Hydrolysate of Ulva australis
by You-An Kang, Ye-Jin Kim, Sang-Keun Jin and Hwa-Jung Choi
Mar. Drugs 2023, 21(9), 469; https://doi.org/10.3390/md21090469 - 26 Aug 2023
Cited by 4 | Viewed by 1903
Abstract
The protein extract of Ulva australis hydrolyzed with Alcalase and Flavourzyme was found to have multi-functional properties, including total antioxidant capacity (TAC), collagenase inhibitory, and antibacterial activities. The #5 fraction (SP5) and #7 fraction (SP7) of U. australis hydrolysate from cation-exchange chromatography displayed [...] Read more.
The protein extract of Ulva australis hydrolyzed with Alcalase and Flavourzyme was found to have multi-functional properties, including total antioxidant capacity (TAC), collagenase inhibitory, and antibacterial activities. The #5 fraction (SP5) and #7 fraction (SP7) of U. australis hydrolysate from cation-exchange chromatography displayed significantly high TAC, collagenase inhibitory, and antibacterial effects against Propionibacterium acnes, and only the Q3 fraction from anion-exchange chromatography displayed high multi-functional activities. Eight of 42 peptides identified by MALDI-TOF/MS and Q-TOF/MS/MS were selected from the results for screening with molecular docking on target proteins and were then synthesized. Thr-Gly-Thr-Trp (TGTW) displayed ABTS [2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid)] radical scavenging activity. The effect of TAC as Trolox equivalence was dependent on the concentration of TGTW. Asn-Arg-Asp-Tyr (NRDY) and Arg-Asp-Arg-Phe (RDRF) exhibited collagenase inhibitory activity, which increased according to the increase in concentration, and their IC50 values were 0.95 mM and 0.84 mM, respectively. Peptides RDRF and His-Ala-Val-Tyr (HAVY) displayed anti-P. Acnes effects, with IC50 values of 8.57 mM and 13.23 mM, respectively. These results suggest that the U. australis hydrolysate could be a resource for the application of effective nutraceuticals and cosmetics. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential IV)
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15 pages, 4559 KiB  
Article
Peptidomics Analysis Reveals the Buccal Gland of Jawless Vertebrate Lamprey as a Source of Multiple Bioactive Peptides
by Yaocen Wang, Feng Sun, Zhuoying Wang, Xuyuan Duan, Qingwei Li, Yue Pang and Meng Gou
Mar. Drugs 2023, 21(7), 389; https://doi.org/10.3390/md21070389 - 29 Jun 2023
Cited by 1 | Viewed by 1378
Abstract
Various proteins with antibacterial, anticoagulant, and anti-inflammatory properties have been identified in the buccal glands of jawless blood-sucking vertebrate lampreys. However, studies on endogenous peptides in the buccal gland of lampreys are limited. In this study, 4528 endogenous peptides were identified from 1224 [...] Read more.
Various proteins with antibacterial, anticoagulant, and anti-inflammatory properties have been identified in the buccal glands of jawless blood-sucking vertebrate lampreys. However, studies on endogenous peptides in the buccal gland of lampreys are limited. In this study, 4528 endogenous peptides were identified from 1224 precursor proteins using peptidomics and screened for bioactivity in the buccal glands of the lamprey, Lethenteron camtschaticum. We synthesized four candidate bioactive peptides (VSLNLPYSVVRGEQFVVQA, DIPVPEVPILE, VVQLPPVVLGTFG, and VPPPPLVLPPASVK), calculated their secondary structures, and validated their bioactivity. The results showed that the peptide VSLNLPYSVVRGEQFVVQA possessed anti-inflammatory activity, which significantly increased the expression of anti-inflammatory factors and decreased the expression of inflammatory factors in THP-1 cells. The peptide VVQLPPVVLGTFG showed antibacterial activity against some gram-positive bacteria. The peptide VSLNLPYSVVRGEQFVQA possessed good ACE inhibitory activity at low concentrations, but no dose-related correlation was observed. Our study revealed that the buccal glands of the jawless vertebrate lamprey are a source of multiple bioactive peptides, which will provide new insights into the blood-sucking mechanism of lamprey. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential IV)
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Review

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37 pages, 2511 KiB  
Review
Marine Invertebrate Antimicrobial Peptides and Their Potential as Novel Peptide Antibiotics
by Svetlana V. Guryanova, Sergey V. Balandin, Oksana Yu. Belogurova-Ovchinnikova and Tatiana V. Ovchinnikova
Mar. Drugs 2023, 21(10), 503; https://doi.org/10.3390/md21100503 - 23 Sep 2023
Cited by 9 | Viewed by 4971
Abstract
Marine invertebrates constantly interact with a wide range of microorganisms in their aquatic environment and possess an effective defense system that has enabled their existence for millions of years. Their lack of acquired immunity sets marine invertebrates apart from other marine animals. Invertebrates [...] Read more.
Marine invertebrates constantly interact with a wide range of microorganisms in their aquatic environment and possess an effective defense system that has enabled their existence for millions of years. Their lack of acquired immunity sets marine invertebrates apart from other marine animals. Invertebrates could rely on their innate immunity, providing the first line of defense, survival, and thriving. The innate immune system of marine invertebrates includes various biologically active compounds, and specifically, antimicrobial peptides. Nowadays, there is a revive of interest in these peptides due to the urgent need to discover novel drugs against antibiotic-resistant bacterial strains, a pressing global concern in modern healthcare. Modern technologies offer extensive possibilities for the development of innovative drugs based on these compounds, which can act against bacteria, fungi, protozoa, and viruses. This review focuses on structural peculiarities, biological functions, gene expression, biosynthesis, mechanisms of antimicrobial action, regulatory activities, and prospects for the therapeutic use of antimicrobial peptides derived from marine invertebrates. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential IV)
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21 pages, 4498 KiB  
Review
Marine Organisms as a Prolific Source of Bioactive Depsipeptides
by Mingyuan Zeng, Jianyun Tao, Shuang Xu, Xuelian Bai and Huawei Zhang
Mar. Drugs 2023, 21(2), 120; https://doi.org/10.3390/md21020120 - 11 Feb 2023
Cited by 14 | Viewed by 2510
Abstract
Depsipeptides, an important group of polypeptides containing residues of hydroxy acids and amino acids linked together by amide and ester bonds, have potential applications in agriculture and medicine. A growing body of evidence demonstrates that marine organisms are prolific sources of depsipeptides, such [...] Read more.
Depsipeptides, an important group of polypeptides containing residues of hydroxy acids and amino acids linked together by amide and ester bonds, have potential applications in agriculture and medicine. A growing body of evidence demonstrates that marine organisms are prolific sources of depsipeptides, such as marine cyanobacteria, sponges, mollusks, microorganisms and algae. However, these substances have not yet been comprehensively summarized. In order to enrich our knowledge about marine depsipeptides, their biological sources and structural features, as well as bioactivities, are highlighted in this review after an extensive literature search and data analysis. Full article
(This article belongs to the Special Issue Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential IV)
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