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Marine Proteins: Biological Activities and Applications

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: 15 July 2026 | Viewed by 1823

Special Issue Editor


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Guest Editor
Department of Chemistry, Pukyong National University, Busan 48513, Republic of Korea
Interests: cold-active enzymes; psychrophilic proteins; ice-binding proteins; antifreeze proteins; cold-adaptation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

We are excited to announce this Special Issue dedicated to “Marine Proteins: Biological Activities and Applications”. The vast and diverse marine environment represents an extraordinary reservoir of unique proteins, each offering distinct structures and functions. These marine-derived proteins hold immense promise, exhibiting a wide array of biological activities that are highly sought after across various sectors, from healthcare to industrial innovation.

This Special Issue aims to gather cutting-edge research and comprehensive reviews on marine proteins in their entirety. We welcome submissions that cover their isolation, characterization, and the exploration of their diverse biological properties—including, but not limited to, antimicrobial, antioxidant, anti-inflammatory, and enzymatic activities. Furthermore, we encourage contributions showcasing their practical applications in pharmaceuticals, functional foods, cosmetics, and other biotechnological fields. Join us in illuminating the remarkable potential and versatility of proteins found within our oceans.

Prof. Dr. Hak Jun Kim
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 250 words) can be sent to the Editorial Office for assessment.

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 proteins
  • biological activities
  • biotechnological applications
  • marine-derived bioactive
  • marine enzymes
  • functional foods
  • pharmaceuticals
  • cosmeceuticals
  • protein characterization
  • sustainable biorefineries

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Published Papers (2 papers)

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Research

27 pages, 17337 KB  
Article
Identification, Screening and Mechanism Analysis of Anti-Parkinson’s Disease Peptides from Rapana venosa Protein Hydrolysates
by Qingzhong Wang, Shuqin Shao, Yizhuo Wang, Wenshuai Fan, Zilong Wang, Xuchang Liu, Kechun Liu and Shanshan Zhang
Mar. Drugs 2026, 24(5), 180; https://doi.org/10.3390/md24050180 - 15 May 2026
Viewed by 461
Abstract
At present, there is still a lack of effective treatments to slow the progression of Parkinson’s disease. Naturally derived active substances, valued for their safety and multi-target potential, have become an important direction in anti-PD drug development, with marine organisms representing a valuable [...] Read more.
At present, there is still a lack of effective treatments to slow the progression of Parkinson’s disease. Naturally derived active substances, valued for their safety and multi-target potential, have become an important direction in anti-PD drug development, with marine organisms representing a valuable source of bioactive peptides. This study aimed to isolate and identify anti-PD peptides from Rapana venosa protein hydrolysates. Through bioactivity-guided screening combined with an MPTP-induced zebrafish PD model, three novel active peptides—KSTELLI, FLVKLPMFM, and SDSLSEILIS—were successfully identified. The study showed that these peptides significantly alleviated dopaminergic neuron loss, improved the cerebral vascular system, restored motor and sensory function, and alleviated oxidative stress. Molecular docking confirmed their stable binding to key PD targets (DDC, α-synuclein, and MAO-B). Further transcriptomic and gene expression analyses revealed that their neuroprotective effects involve the regulation of pathways related to metabolism, oxidative stress, inflammation, and apoptosis, with the three peptides exhibiting distinct mechanistic emphases. The research demonstrates that these marine-derived peptides exert neuroprotective effects through a synergistic multi-target mechanism, laying a foundation for the development of novel lead compounds against Parkinson’s disease. Full article
(This article belongs to the Special Issue Marine Proteins: Biological Activities and Applications)
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21 pages, 3233 KB  
Article
Macroalgal Peptides with Predicted α-Glucosidase Inhibitory Activity: Preparation and Molecular Docking
by Sakhi Ghelichi, Seyed Hossein Helalat, Mona Hajfathalian, Birte Svensson and Charlotte Jacobsen
Mar. Drugs 2026, 24(3), 91; https://doi.org/10.3390/md24030091 - 26 Feb 2026
Cited by 1 | Viewed by 873
Abstract
This study investigated the α-glucosidase inhibitory potential of enzymatic/alkaline treatments from Palmaria palmata using different proteases and pairwise combinations thereof. Treatments prepared with Alcalase®, Flavourzyme®, and Formea® Prime, alone or in combination, were evaluated for dose-dependent inhibitory activity. [...] Read more.
This study investigated the α-glucosidase inhibitory potential of enzymatic/alkaline treatments from Palmaria palmata using different proteases and pairwise combinations thereof. Treatments prepared with Alcalase®, Flavourzyme®, and Formea® Prime, alone or in combination, were evaluated for dose-dependent inhibitory activity. Alcalase®-derived treatments exhibited the highest α-glucosidase inhibition, achieving an IC50 of 2.48 mg·mL−1, outperforming other treatments and combinations. Membrane fractionation of the Alcalase®-derived treatment into >5 kDa, 3–5 kDa, 1–3 kDa, and <1 kDa fractions revealed a size-dependent trend, with the <1 kDa fraction showing the strongest inhibition (IC50 of 1.94 mg·mL−1). Three peptides, RADIPFRRA, DGIAEAWLG, and FWSQIFGVAF, from the <1 kDa fraction were identified as potential α-glucosidase inhibitors using the BIOPEP-UWM database and were further selected based on a Peptide Ranker score above 0.6 for in silico docking analyses. Docking revealed distinct binding modes: RADIPFRRA and DGIAEAWLG occupied the catalytic cleft, interacting with key residues (Asp518, Asp616, Trp481, Trp613) consistent with competitive inhibition, whereas FWSQIFGVAF bound to a peripheral site, suggesting potential allosteric modulation. Physicochemical analysis further highlighted differences in charge and isoelectric point correlating with their binding behavior. Together, these findings demonstrate that low-molecular-weight peptides derived from P. palmata proteins, particularly those generated by Alcalase®, possess significant α-glucosidase inhibitory activity, and provide structural insights for the rational design of peptide-based modulators of carbohydrate metabolism. Full article
(This article belongs to the Special Issue Marine Proteins: Biological Activities and Applications)
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