The Bioactive Potential of Marine-Derived Peptides and Proteins

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: 31 December 2024 | Viewed by 3817

Special Issue Editors


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Guest Editor
Research Group for Bioactives—Analysis and Application, National Food Institute, Technical University of Denmark, 2800 Kongens Lyngby, Denmark
Interests: protein hydrolysis; bioactive compounds; antioxidants; lipid oxidation; peptide purification and characterization; marine protein and oil; algae proteins and polyphenols; marine side-streams; functional foods; pharmaceuticals and nutraceuticals; emulsions

E-Mail Website
Guest Editor
Research Group for Bioactives—Analysis and Application, National Food Institute, Technical University of Denmark, 2800 Kongens Lyngby, Denmark
Interests: antioxidants, bioactive compounds, protein hydrolysis, functional foods, emulsions, marine protein and oil, emulsions, marine biomasses and underutilized marine biomasses, lipid oxidation
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Special Issue Information

Dear Colleagues,

Marine ecosystems host organisms that are a treasure trove of bioactive compounds, including bioactive peptides and proteins. These molecules exhibit significant potential for various applications, including antioxidants, antihypertensives, and anti-obesity agents, among others. Therefore, it is crucial to give special attention to marine-based proteins and peptides in relation to their bioactive properties, finding sustainable and natural substitutes for chemical compounds.

In this Special Issue, we focus on the latest advancements concerning the discovery, characterization, and utilization of bioactive peptides and proteins derived from marine sources. Our objective is to explore their bioactive properties across diverse contexts, investigating their roles in nutrition, functional foods, beverages, pharmaceuticals, nutraceuticals, and biotechnology, emphasizing their distinctive properties and associated benefits. Therefore, we invite academic and industrial scientists and researchers to submit their research and review articles, contributing to a comprehensive understanding of these marine bioactive compounds and fostering further innovation in this promising field.

Dr. Sakhi Ghelichi 
Dr. Ann-Dorit Moltke Sørensen
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.

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Keywords

  • marine bioactive proteins and peptides
  • fish, algae, and marine side-stream
  • antioxidants
  • enzymatic treatments and protein hydrolysates
  • peptide purification and characterization
  • antimicrobial properties
  • antihypertensive properties
  • anti-obesity and anti-diabetic properties
  • anticancer properties
  • anti-inflammatory properties

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Published Papers (3 papers)

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Research

19 pages, 8961 KiB  
Article
Novel Insights into Ethanol-Soluble Oyster Peptide–Zinc-Chelating Agents: Structural Characterization, Chelation Mechanism, and Potential Protection on MEHP-Induced Leydig Cells
by Zhen Lu, Qianqian Huang, Xiaoming Qin, Fujia Chen, Enzhong Li and Haisheng Lin
Mar. Drugs 2024, 22(10), 465; https://doi.org/10.3390/md22100465 - 10 Oct 2024
Viewed by 1114
Abstract
Numerous studies have reported that mono-(2-ethylhexyl) phthalate (MEHP) (bioactive metabolite of Di(2-ethylhexyl) phthalate) has inhibitory effects on Leydig cells. This study aims to prepare an oyster peptide–zinc complex (PEP-Zn) to alleviate MEHP-induced damage in Leydig cells. Zinc-binding peptides were obtained through the following [...] Read more.
Numerous studies have reported that mono-(2-ethylhexyl) phthalate (MEHP) (bioactive metabolite of Di(2-ethylhexyl) phthalate) has inhibitory effects on Leydig cells. This study aims to prepare an oyster peptide–zinc complex (PEP-Zn) to alleviate MEHP-induced damage in Leydig cells. Zinc-binding peptides were obtained through the following processes: zinc-immobilized affinity chromatography (IMAC-Zn2+), liquid chromatography–mass spectrometry technology (LC-MS/MS) analysis, molecular docking, molecular dynamic simulation, and structural characterization. Then, the Zn-binding peptide (PEP) named Glu—His—Ala—Pro—Asn—His—Asp—Asn—Pro—Gly—Asp—Leu (EHAPNHDNPGDL) was identified. EHAPNHDNPGDL showed the highest zinc-chelating ability of 49.74 ± 1.44%, which was higher than that of the ethanol-soluble oyster peptides (27.50 ± 0.41%). In the EHAPNHDNPGDL-Zn complex, Asn-5, Asp-7, Asn-8, His-2, and Asp-11 played an important role in binding to the zinc ion. Additionally, EHAPNHDNPGDL-Zn was found to increase the cell viability, significantly increase the relative activity of antioxidant enzymes and testosterone content, and decrease malondialdehyde (MDA) content in MEHP-induced TM3 cells. The results also indicated that EHAPNHDNPGDL-Zn could alleviate MEHP-induced apoptosis by reducing the protein level of p53, p21, and Bax, and increasing the protein level of Bcl-2. These results indicate that the zinc-chelating peptides derived from oyster peptides could be used as a potential dietary zinc supplement. Full article
(This article belongs to the Special Issue The Bioactive Potential of Marine-Derived Peptides and Proteins)
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15 pages, 3632 KiB  
Article
Glutamic-Alanine Rich Glycoprotein from Undaria pinnatifida: A Promising Natural Anti-Inflammatory Agent
by Md Saifur Rahman, Md Badrul Alam, Marufa Naznin, Mst Hur Madina and S. M. Rafiquzzaman
Mar. Drugs 2024, 22(9), 383; https://doi.org/10.3390/md22090383 - 26 Aug 2024
Viewed by 974
Abstract
This study aimed to assess the anti-inflammatory properties of a bioactive glutamic-alanine rich glycoprotein (GP) derived from Undaria pinnatifida on both LPS-stimulated RAW264.7 cells, peritoneal macrophages, and mouse models of carrageenan- and xylene-induced inflammation, investigating the underlying molecular mechanisms. In both in-vitro and [...] Read more.
This study aimed to assess the anti-inflammatory properties of a bioactive glutamic-alanine rich glycoprotein (GP) derived from Undaria pinnatifida on both LPS-stimulated RAW264.7 cells, peritoneal macrophages, and mouse models of carrageenan- and xylene-induced inflammation, investigating the underlying molecular mechanisms. In both in-vitro and in-vivo settings, GP was found to reduce the expression of inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2) while also inhibiting the production of nitric oxide (NO) and prostaglandin E2 (PGE2) in response to lipopolysaccharide (LPS) stimulation. GP treatment significantly impeded the nuclear translocation of the nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) pathway by blocking the phosphorylation of IKKα and IκBα, leading to a reduction in proinflammatory cytokines such as tumor necrosis factor-α (TNF-α), interleukin-1β (IL-1β), and interleukin-6 (IL-6). Additionally, GP effectively inhibited the activation of mitogen-activated protein kinases (MAPKs), with specific inhibitors of p38 and extra-cellular signal regulated kinase (ERK) enhancing GP’s anti-inflammatory efficacy. Notably, GP administration at 10 mg/kg/day (p.o.) markedly reduced carrageenan-induced paw inflammation and xylene-induced ear edema by preventing the infiltration of inflammatory cells into targeted tissues. GP treatment also downregulated key inflammatory markers, including iNOS, COX-2, IκBα, and NF-κB, by suppressing the phosphorylation of p38 and ERK, thereby improving the inflammatory index in both carrageenan- and xylene-induced mouse models. These findings suggest that marine resources, particularly seaweeds like U. pinnatifida, could serve as valuable sources of natural anti-inflammatory proteins for the effective treatment of inflammation and related conditions. Full article
(This article belongs to the Special Issue The Bioactive Potential of Marine-Derived Peptides and Proteins)
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21 pages, 6311 KiB  
Article
Investigation of Antioxidant Activity of Protein Hydrolysates from New Zealand Commercial Low-Grade Fish Roes
by Shuxian Li, Alan Carne and Alaa El-Din Ahmed Bekhit
Mar. Drugs 2024, 22(8), 364; https://doi.org/10.3390/md22080364 - 11 Aug 2024
Viewed by 1416
Abstract
The objective of this study was to investigate the nutrient composition of low-grade New Zealand commercial fish (Gemfish and Hoki) roe and to investigate the effects of delipidation and freeze-drying processes on roe hydrolysis and antioxidant activities of their protein hydrolysates. Enzymatic hydrolysis [...] Read more.
The objective of this study was to investigate the nutrient composition of low-grade New Zealand commercial fish (Gemfish and Hoki) roe and to investigate the effects of delipidation and freeze-drying processes on roe hydrolysis and antioxidant activities of their protein hydrolysates. Enzymatic hydrolysis of the Hoki and Gemfish roe homogenates was carried out using three commercial proteases: Alcalase, bacterial protease HT, and fungal protease FP-II. The protein and lipid contents of Gemfish and Hoki roes were 23.8% and 7.6%; and 17.9% and 10.1%, respectively. The lipid fraction consisted mainly of monounsaturated fatty acid (MUFA) in both Gemfish roe (41.5%) and Hoki roe (40.2%), and docosahexaenoic (DHA) was the dominant polyunsaturated fatty acid (PUFA) in Gemfish roe (21.4%) and Hoki roe (18.6%). Phosphatidylcholine was the main phospholipid in Gemfish roe (34.6%) and Hoki roe (28.7%). Alcalase achieved the most extensive hydrolysis, and its hydrolysate displayed the highest 2,2-dipheny1-1-picrylhydrazyl (DPPH)˙ and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activities and ferric reducing antioxidant power (FRAP). The combination of defatting and freeze-drying treatments reduced DPPH˙ scavenging activity (by 38%), ABTS˙ scavenging activity (by 40%) and ferric (Fe3+) reducing power by18% (p < 0.05). These findings indicate that pre-processing treatments of delipidation and freeze-drying could negatively impact the effectiveness of enzymatic hydrolysis in extracting valuable compounds from low grade roe. Full article
(This article belongs to the Special Issue The Bioactive Potential of Marine-Derived Peptides and Proteins)
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