Bioactive Proteins and Peptides from Marine Mollusks

A special issue of Marine Drugs (ISSN 1660-3397). This special issue belongs to the section "Marine-Derived Ingredients for Drugs, Cosmeceuticals and Nutraceuticals".

Deadline for manuscript submissions: closed (28 February 2025) | Viewed by 6655

Special Issue Editor


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Guest Editor
South China Seas Institute of Oceanography, Chinese Academy of Sciences, Guangzhou, China
Interests: proteins; peptides; marine mollusks; gastropoda; bivalvia; cephalopoda

Special Issue Information

Dear Colleagues,

The vast biodiversity among marine mollusks, alongside their significant utility and high nutritional value, has aroused great interest in the scientific community.

Many novel biomolecules originating from marine mollusks have been chemically determined and examples include proteins, peptides, fatty acids, terpenes, steroids, polyketides and nitrogen-containing compounds. These biologically active compounds from marine mollusks present great pharmacological potential in terms of their antioxidant, antibacterial, antiviral, antitumor, neuroprotective, and immunostimulating effects.

Among mollusk-derived natural products, protein and peptide-based therapeutics are a rapidly expanding category of pharmaceutical agents that are currently being exploited to treat various diseases. The high specificity and low toxicity of protein and peptide molecules compared to other small molecules make them a focus for drug development, with extensive research already underway on their therapeutic value.

This Special Issue has been developed to synthesize the latest research findings on various biomedical applications of proteins and peptides derived from diverse marine mollusks. We invite submissions of original research articles as well as comprehensive reviews in this field.

Dr. Yang Zhang
Guest Editor

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Keywords

  • proteins
  • peptides
  • marine mollusks
  • gastropoda
  • bivalvia
  • cephalopoda

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Published Papers (4 papers)

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Research

16 pages, 3962 KiB  
Article
Ark Shell-Derived Peptides AWLNH (P3) and PHDL (P4) Mitigate Foam Cell Formation by Modulating Cholesterol Metabolism and HO-1/Nrf2-Mediated Oxidative Stress in Atherosclerosis
by Chathuri Kaushalya Marasinghe and Jae-Young Je
Mar. Drugs 2025, 23(3), 111; https://doi.org/10.3390/md23030111 - 5 Mar 2025
Viewed by 793
Abstract
Atherosclerosis, a leading contributor to cardiovascular diseases (CVDs), is characterized by foam cell formation driven by excessive lipid accumulation in macrophages and vascular smooth muscle cells. This study elucidates the anti-atherosclerotic potential of AWLNH (P3) and PHDL (P4) peptides by assessing their effects [...] Read more.
Atherosclerosis, a leading contributor to cardiovascular diseases (CVDs), is characterized by foam cell formation driven by excessive lipid accumulation in macrophages and vascular smooth muscle cells. This study elucidates the anti-atherosclerotic potential of AWLNH (P3) and PHDL (P4) peptides by assessing their effects on foam cell formation, lipid metabolism, and oxidative stress regulation. P3 and P4 effectively suppressed intracellular lipid accumulation in RAW264.7 macrophages and human aortic smooth muscle cells (hASMCs), thereby mitigating foam cell formation. Mechanistically, both peptides modulated cholesterol homeostasis by downregulating cholesterol influx mediators, cluster of differentiation 36 (CD36), and class A1 scavenger receptor (SR-A1), while upregulating cholesterol efflux transporters ATP-binding cassette subfamily A member 1 (ABCA1) and ATP-binding cassette subfamily G member 1 (ABCG1). The activation of peroxisome proliferator-activated receptor-gamma (PPAR-γ) and liver X receptor-alpha (LXR-α) further substantiated their role in promoting cholesterol efflux and restoring lipid homeostasis. Additionally, P3 and P4 peptides exhibited potent antioxidative properties by attenuating reactive oxygen species (ROS) generation through activation of the HO-1/Nrf2 signaling axis. HO-1 silencing via siRNA transfection abolished these effects, confirming HO-1-dependent regulation of oxidative stress and lipid metabolism. Collectively, these findings highlight P3 and P4 peptides as promising therapeutic agents for atherosclerosis by concurrently targeting foam cell formation, cholesterol dysregulation, and oxidative stress, warranting further exploration for potential clinical applications. Full article
(This article belongs to the Special Issue Bioactive Proteins and Peptides from Marine Mollusks)
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20 pages, 4758 KiB  
Article
Integrated Macrogenomics and Metabolomics Analysis of the Effect of Sea Cucumber Ovum Hydrolysates on Dextran Sodium Sulfate-Induced Colitis
by Shunmin Gong, Liqin Sun, Yongjun Sun, Wenming Ju, Gongming Wang, Jian Zhang, Xuejun Fu, Chang Lu, Yu Zhang, Wenkui Song, Mingbo Li and Leilei Sun
Mar. Drugs 2025, 23(2), 73; https://doi.org/10.3390/md23020073 - 7 Feb 2025
Viewed by 774
Abstract
Inflammatory bowel disease remains a significant challenge in clinical settings. This study investigated the therapeutic potential of sea cucumber ovum hydrolysates (SCH) in a dextran sulfate sodium (DSS)-induced colitis mouse model. SCH, defined by its elevated stability and solubility, with a molecular weight [...] Read more.
Inflammatory bowel disease remains a significant challenge in clinical settings. This study investigated the therapeutic potential of sea cucumber ovum hydrolysates (SCH) in a dextran sulfate sodium (DSS)-induced colitis mouse model. SCH, defined by its elevated stability and solubility, with a molecular weight below 1000 Da, significantly alleviated DSS-induced colitis, as evidenced by enhanced splenic index, reduced colonic damage, and diminished serum pro-inflammatory cytokines. Furthermore, macrogenomic analysis demonstrated that SCH increased beneficial gut microbes and decreased pro-inflammatory bacteria. Furthermore, metabolomic analysis of colonic tissues identified elevated levels of anti-inflammatory metabolites, such as Phenyllactate, 2-Hydroxyglutarate, and L-Aspartic acid, in colitis mice after oral administration of SCH. In conclusion, SCH represents a promising candidate for the treatment of colitis. Full article
(This article belongs to the Special Issue Bioactive Proteins and Peptides from Marine Mollusks)
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14 pages, 11931 KiB  
Article
Machine Learning-Driven Discovery and Evaluation of Antimicrobial Peptides from Crassostrea gigas Mucus Proteome
by Jingchen Song, Kelin Liu, Xiaoyang Jin, Ke Huang, Shiwei Fu, Wenjie Yi, Yijie Cai, Ziniu Yu, Fan Mao and Yang Zhang
Mar. Drugs 2024, 22(9), 385; https://doi.org/10.3390/md22090385 - 26 Aug 2024
Cited by 1 | Viewed by 2353
Abstract
Marine antimicrobial peptides (AMPs) represent a promising source for combating infections, especially against antibiotic-resistant pathogens and traditionally challenging infections. However, traditional drug discovery methods face challenges such as time-consuming processes and high costs. Therefore, leveraging machine learning techniques to expedite the discovery of [...] Read more.
Marine antimicrobial peptides (AMPs) represent a promising source for combating infections, especially against antibiotic-resistant pathogens and traditionally challenging infections. However, traditional drug discovery methods face challenges such as time-consuming processes and high costs. Therefore, leveraging machine learning techniques to expedite the discovery of marine AMPs holds significant promise. Our study applies machine learning to develop marine AMPs, focusing on Crassostrea gigas mucus rich in antimicrobial components. We conducted proteome sequencing of C. gigas mucous proteins, used the iAMPCN model for peptide activity prediction, and evaluated the antimicrobial, hemolytic, and cytotoxic capabilities of six peptides. Proteomic analysis identified 4490 proteins, yielding about 43,000 peptides (8–50 amino acids). Peptide ranking based on length, hydrophobicity, and charge assessed antimicrobial potential, predicting 23 biological activities. Six peptides, distinguished by their high relative scores and promising biological activities, were chosen for bactericidal assay. Peptides P1 to P4 showed antimicrobial activity against E. coli, with P2 and P4 being particularly effective. All peptides inhibited S. aureus growth. P2 and P4 also exhibited significant anti-V. parahaemolyticus effects, while P1 and P3 were non-cytotoxic to HEK293T cells at detectable concentrations. Minimal hemolytic activity was observed for all peptides even at high concentrations. This study highlights the potent antimicrobial properties of naturally occurring oyster mucus peptides, emphasizing their low cytotoxicity and lack of hemolytic effects. Machine learning accurately predicted biological activity, showcasing its potential in peptide drug discovery. Full article
(This article belongs to the Special Issue Bioactive Proteins and Peptides from Marine Mollusks)
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24 pages, 16330 KiB  
Article
Prokaryotic Expression, Purification, and Biological Properties of a Novel Bioactive Protein (PFAP-1) from Pinctada fucata
by Peng Liu, Wenyue Li, Jianbing Liu, Xiaojian Mo, Jiaxing Tang and Jiang Lin
Mar. Drugs 2024, 22(8), 345; https://doi.org/10.3390/md22080345 - 27 Jul 2024
Cited by 2 | Viewed by 2130
Abstract
Pinctada fucata meat is the main by-product of the pearl harvesting industry. It is rich in nutrition, containing a lot of protein and peptides, and holds significant value for both medicine and food. In this study, a new active protein was discovered and [...] Read more.
Pinctada fucata meat is the main by-product of the pearl harvesting industry. It is rich in nutrition, containing a lot of protein and peptides, and holds significant value for both medicine and food. In this study, a new active protein was discovered and expressed heterogeneously through bioinformatics analysis. It was then identified using Western blot, molecular weight, and mass spectrometry. The antibacterial activity, hemolysis activity, antioxidant activity, and Angiotensin-Converting Enzyme II (ACE2) inhibitory activity were investigated. An unknown functional protein was screened through the Uniprot protein database, and its primary structure did not resemble existing proteins. It was an α-helical cationic polypeptide we named PFAP-1. The codon-optimized full-length PFAP-1 gene was synthesized and inserted into the prokaryotic expression vector pET-30a. The induced expression conditions were determined with a final isopropyl-β-d-thiogalactoside (IPTG) concentration of 0.2 mM, an induction temperature of 15 °C, and an induction time of 16 h. The recombinant PFAP-1 protein, with low endotoxin and sterility, was successfully prepared. The recombinant PFAP-1 protein exhibited strong antibacterial activity against methicillin-resistant Staphylococcus aureus (MRSA) in vitro, and the diameter of the inhibition zone was 15.99 ± 0.02 mm. Its minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) were 37.5 μg/mL and 150 μg/mL, respectively, and its hemolytic activity was low (11.21%) at the bactericidal concentration. The recombinant PFAP-1 protein significantly inhibited the formation of MRSA biofilm and eradicated MRSA biofilm. It also demonstrated potent 1,1-diphenyl-2-picryl-hydrazyl radical (DPPH) scavenging activity with a half-maximal inhibitory concentration (IC50) of 40.83 μg/mL. The IC50 of ACE2 inhibition was 5.66 μg/mL. Molecular docking results revealed that the optimal docking fraction of PFAP-1 protein and ACE2 protein was −267.78 kcal/mol, with a confidence level of 0.913. The stable binding complex was primarily formed through nine groups of hydrogen bonds, three groups of salt bridges, and numerous hydrophobic interactions. In conclusion, recombinant PFAP-1 can serve as a promising active protein in food, cosmetics, or medicine. Full article
(This article belongs to the Special Issue Bioactive Proteins and Peptides from Marine Mollusks)
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