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9.6
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Marine Drugs
Special Issues
Bioactive Proteins and Peptides from Marine Mollusks
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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: 28 February 2025 | Viewed by 3250

Special Issue Editor

Dr. Yang Zhang

E-Mail Website
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

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

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

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Further information on MDPI's Special Issue polices can be found here.

Published Papers (2 papers)

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Research

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
Viewed by 1391
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
Viewed by 1556
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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