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The Bioactive Potential of Marine-Derived Peptides and Proteins

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A special issue of Marine Drugs (ISSN 1660-3397). This special issue belongs to the section "Marine Pharmacology".

Deadline for manuscript submissions: 31 July 2025 | Viewed by 9246

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Dr. Sakhi Ghelichi

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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

Dr. Ann-Dorit Moltke Sørensen

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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: 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

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 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 (7 papers)

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Research

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20 pages, 4912 KiB

Open AccessArticle

Ameliorative Effect of Sipunculus nudus Hydrolysate on Cisplatin-Induced Nephrotoxicity by Mitigating Oxidative Stress, Inflammation and Apoptosis

by Susu Tao, Yi Qi, Jialong Gao, Huafang Yuan, Ruimin Wang, Xiaoqin Shen, Gang Wei and Zhilan Peng

Mar. Drugs 2025, 23(3), 100; https://doi.org/10.3390/md23030100 - 24 Feb 2025

Viewed by 546

Abstract

The present study investigated the protective effects and possible mechanisms of an ultrafiltration fraction of Sipunculus nudus hydrolysate (UFSH) on cisplatin-induced kidney damage in a mouse model. The results showed that UFSH significantly attenuated cisplatin-induced nephrotoxicity by inhibiting increases in blood urea nitrogen (BUN) and serum creatinine (SCr). Additionally, UFSH treatment significantly alleviated cisplatin-induced renal histopathological changes, such as significant dilation of renal tubules, cast formation, and tubular cell necrosis, as well as tubulointerstitial fibrosis. Moreover, UFSH decreased cisplatin-induced oxidative stress by increasing the activities of antioxidant enzymes SOD and GSH-Px, while reducing the malondialdehyde (MDA) level in the kidney. Furthermore, UFSH significantly inhibited cisplatin-induced increases in inflammatory cytokines, including Interleukin 1-beta (IL-1β), Interleukin-6 (IL-6), and Tumor necrosis factor-alpha (TNF-α). Western blotting revealed that UFSH inhibited the phosphorylation of the inflammation-associated MAPK/NF-κB signaling pathway, lowered the expression of the apoptosis-related protein Bax, and reversed the reduction in the anti-apoptotic Bcl-2 protein. This investigation demonstrated that UFSH can ameliorate cisplatin-induced nephrotoxicity by mitigating oxidative stress, inflammation, and apoptosis. Full article

(This article belongs to the Special Issue The Bioactive Potential of Marine-Derived Peptides and Proteins)

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22 pages, 8432 KiB

Open AccessArticle

Antioxidant Peptides from Miiuy Croaker Swim Bladders: Ameliorating Effect and Mechanism in NAFLD Cell Model through Regulation of Hypolipidemic and Antioxidant Capacity

by Yu-Mei Wang, Ming-Xue Ge, Su-Zhen Ran, Xin Pan, Chang-Feng Chi and Bin Wang

Mar. Drugs 2025, 23(2), 63; https://doi.org/10.3390/md23020063 - 1 Feb 2025

Cited by 1 | Viewed by 1016

Abstract

In this work, the hypolipidemic and antioxidative capacity of FSGLR (S7) and GIEWA (S10) from miiuy croaker swim bladders was explored systematically in an oleic acid (OA)-induced nonalcoholic fatty liver disease (NAFLD) model of HepG2 cells. Moreover, the hypolipidemic activity of S7 and S10 and their antioxidative abilities were preliminarily investigated in combination with molecular docking technology. The results indicated that S7 and S10 could decrease the amount of lipid accumulation and the content of triglycerides (TG) and total cholesterol (TC) in the OA-induced NAFLD cell model in a dose-dependent manner. In addition, S7 and S10 exhibited better bile salt binding, pancreatic lipase (PL) inhibition, and cholesterol esterase (CE) inhibition capacities. The hypolipidemic mechanisms of S7 and S10 were connected with the downregulation of the mRNA expression levels of adipogenic factors, including sterol-regulatory element-binding protein-1c (SREBP-1c), acetyl-CoA carboxylase (ACC), sterol-regulatory element-binding protein (SREBP)-2, hydroxymethylglutaryl-CoA reductase (HMGR), and fatty acid synthase (FAS) (p < 0.01), and the upregulation of the mRNA expression of β-oxidation-related factors, including carnitine palmitoyltransferase 1 (CPT-1), acyl-CoA oxidase 1 (ACOX-1), and peroxisome proliferator-activated receptor α (PPARα). Moreover, FSGLR (S7) and GIEWA (S10) could significantly protect HepG2 cells against OA-induced oxidative damage, and their antioxidant mechanisms were related to the increased activity of intracellular antioxidant proteases (superoxide dismutase, SOD; glutathione peroxidase, GSH-PX; catalase, CAT) to remove excess reactive oxygen species (ROS) and decrease the production of malondialdehyde (MDA). The presented findings indicate that the hypolipidemic and antioxidant functions and mechanisms of S7 and S10 could make them potential hypolipidemic and antioxidant candidates for the treatment of NAFLD. Full article

(This article belongs to the Special Issue The Bioactive Potential of Marine-Derived Peptides and Proteins)

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20 pages, 679 KiB

Open AccessArticle

Antioxidant and Anti-Obesity Properties of Acidic and Alkaline Seaweed Extracts Adjusted to Different pH Levels

by Sakhi Ghelichi, Mona Hajfathalian, Sara Falcione and Charlotte Jacobsen

Mar. Drugs 2025, 23(1), 35; https://doi.org/10.3390/md23010035 - 12 Jan 2025

Cited by 1 | Viewed by 1452

Abstract

This research examined antioxidant and anti-obesity effects of Palmaria palmata extracts obtained through acidic or alkaline treatments and subsequent pH adjustments. After two rounds of acidic or alkaline extraction, the extracts were separated from biomass and adjusted to different pH values: for acidic extracts, pH 3 (no adjustment), pH 6, pH 9, and pH 12; for alkaline extracts, pH 12 (no adjustment), pH 9, pH 6, and pH 3. The findings revealed that extraction medium as well as subsequent pH adjustments significantly influenced composition of the extracts in terms of protein content and recovery, amino acids, and phenolic compounds (p < 0.05). Acidic conditions produced extracts with potent radical scavenging, especially at pH 6 (IC₅₀ = 0.30 ± 0.04 mg.mL⁻¹), while alkaline conditions favored metal chelating, with the highest Fe²⁺ chelation at pH 12 (IC₅₀ = 0.65 ± 0.03 mg.mL⁻¹). Moreover, extracts showed inhibitory activities against porcine pancreatic lipase and α-amylase, with the acidic extract at pH 9 showing the best anti-obesity properties (IC₅₀ = 5.38 ± 0.34 mg.mL⁻¹ for lipase and IC₅₀ = 5.79 ± 0.30 mg.mL⁻¹ for α-amylase). However, the highest α-amylase activity was in the alkaline extract at pH 12 (IC₅₀ = 3.05 ± 0.66 mg.mL⁻¹). In conclusion, adjusting the pH of seaweed extracts notably influences their bioactive properties, likely due to changes in the reactivity and interactions of bioactive compounds such as peptides, carbohydrates, and polyphenols. Full article

(This article belongs to the Special Issue The Bioactive Potential of Marine-Derived Peptides and Proteins)

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19 pages, 8961 KiB

Open AccessArticle

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

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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 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

Open AccessArticle

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

Cited by 1 | Viewed by 1396

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 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

Open AccessArticle

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

Cited by 2 | Viewed by 1943

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 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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Review

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48 pages, 2121 KiB

Open AccessReview

Bioactivity of Marine-Derived Peptides and Proteins: A Review

by Fereidoon Shahidi and Abu Saeid

Mar. Drugs 2025, 23(4), 157; https://doi.org/10.3390/md23040157 - 4 Apr 2025

Viewed by 536

Abstract

The marine environment, covering over 70% of the Earth’s surface, serves as a reservoir of bioactive molecules, including peptides and proteins. Due to the unique and often extreme marine conditions, these molecules exhibit distinctive structural features and diverse functional properties, making them promising candidates for therapeutic applications. Marine-derived bioactive peptides, typically consisting of 3 to 40 amino acid residues—though most commonly, 2 to 20—are obtained from parent proteins through chemical or enzymatic hydrolysis, microbial fermentation, or gastrointestinal digestion. Like peptides, protein hydrolysates from collagen, a dominant protein of such materials, play an important role. Peptide bioactivities include antioxidant, antihypertensive, antidiabetic, antimicrobial, anti-inflammatory, anticoagulant, and anti-cancer effects as well as immunoregulatory and wound-healing activities. These peptides exert their effects through mechanisms such as enzyme inhibition, receptor modulation, and free radical scavenging, among others. Fish, algae, mollusks, crustaceans, microbes, invertebrates, and marine by-products such as skin, bones, and viscera are some of the key marine sources of bioactive proteins and peptides. The advancements in the extraction and purification processes, e.g., enzymatic hydrolysis, ultrafiltration, ion-exchange chromatography, high-performance liquid chromatography (HPLC), and molecular docking, facilitate easy identification and purification of such bioactive peptides in greater purity and activity. Despite their colossal potential, their production, scale-up, stability, and bioavailability are yet to be enhanced for industrial applications. Additional work needs to be carried out for optimal extraction processes, to unravel the mechanisms of action, and to discover novel marine sources. This review emphasizes the enormous scope of marine-derived peptides and proteins in the pharmaceutical, nutraceutical, cosmeceutical, and functional food industries, emphasizing their role in health promotion and risk reduction of chronic diseases. Full article

(This article belongs to the Special Issue The Bioactive Potential of Marine-Derived Peptides and Proteins)

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