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A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: 30 November 2026 | Viewed by 6047

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Special Issue Editors

Dr. Yuki Fujii

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Graduate School of Pharmaceutical Sciences, Nagasaki International University, 2825-7 Huis Ten Bosch, Sasebo 859-3298, Japan
Interests: glycobiology; lectins; marine pharmacology; marine invertebrates; signal transduction
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Dr. Marco Gerdol

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Department of Life Sciences, University of Trieste, Via Licio Giorgieri 5, 34127 Trieste, Italy
Interests: immunity; molecular evolution; transcriptome; bivalves; defense peptides
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Prof. Dr. Ogawa Yukiko

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Graduate School of Pharmaceutical Sciences, Nagasaki International University, 2825-7 Huis Ten Bosch, Sasebo 859-3298, Japan
Interests: lectins; mycology; biodefense; anticancer drugs; apoptosis

Prof. Dr. Yasuhiro Ozeki

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Graduate School of NanoBio Sciences, Yokohama City University, 22-2, Seto, Kanazawa-Ku, Yokohama 236-0027, Japan
Interests: lectins; comparative glycomics; glycoevolution; marine invertebrates; glycan-binding characterization
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Special Issue Information

Dear Colleagues,

Marine organisms are rich in glycoconjugates, and their glycans have diverse structures. Glycans are recognized by binding molecules such as lectins, and they regulate cellular functions, but the mechanisms by which they do so remain largely mysterious. In the 2020s, the Human Glycome Project was launched worldwide as a new perspective for the clinic. The project aims to comprehensively analyze human glycan structures and link them to disease onset prediction and advanced medical care. As with the strategy, the time is approaching for marine glycome research to comprehensively elucidate the structures and functions of glycans and related molecules in marine organisms living in various environments, from mid-latitudes to the polar regions. These challenges will elucidate the mechanisms by which marine organisms adapt to the ocean and the potential of these organisms as high-value drug modalities. Techniques that seem relatively distant from traditional glycobiology can potentially significantly advance the marine glycome. We hope to collect articles and reviews with a comparative and interdisciplinary perspective, ranging from genomics to structural biology.

Dr. Yuki Fujii
Dr. Marco Gerdol
Prof. Dr. Ogawa Yukiko
Prof. Dr. Yasuhiro Ozeki
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 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

glycan-drug discovery
lectins
structural glycobiology
transcriptome
glycoconjugates
glycosaminoglycans
deep-sea
glycan-relating enzymes
glycomicrobiology

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Published Papers (5 papers)

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Research

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19 pages, 3404 KB

Open AccessArticle

Floridoside as a Hinge-Targeted Inhibitor of MAPK13: Atomistic Insights from Molecular Dynamics Simulations

by Yang Zhong, Feng Liang, Zhongli Xiong and Zhen Liu

Mar. Drugs 2026, 24(6), 191; https://doi.org/10.3390/md24060191 - 27 May 2026

Abstract

Floridoside (2-(α-D-galactosyl)glycerol) is a compatible solute synthesized in red algae, known for its antioxidant, immunostimulatory, anti-inflammatory, and antimicrobial properties. However, the lack of target validation has limited mechanistic insights into its bioactivity. Mitogen-activated protein kinase 13 (MAPK13), a member of the p38 mitogen-activated protein kinase (p38 MAPK) family with unique structural and functional characteristics, plays an important role in respiratory tissue remodeling, tumor progression, and immune responses, making it an attractive therapeutic target. This study identifies MAPK13 as a high-affinity target of floridoside. In vitro kinase assays validated that floridoside effectively inhibits MAPK13 with a nanomolar inhibitory concentration (IC50 = 13.59 nM), significantly outperforming the classical inhibitor BIRB-796. Unbiased molecular dynamics simulations and steered molecular dynamics simulations reveal that floridoside binds within the MAPK13 hinge region via an ATP-competitive mechanism. Binding free energy analysis combined with computational alanine scanning highlight Asp-113 as a primary interaction hotspot, stabilized by persistent hydrogen bonds with Pro-108 and Met-110. Despite stable complex formation, the flexibility of the glycosidic bond and glycerol tail may limit binding persistence. Comparative simulations with 2-α-glucosylglycerol (2αGG), a stereoisomer of floridoside, demonstrate the sensitivity of MAPK13 binding to subtle structural variations. These findings elucidate the atomistic basis for floridoside’s bioactivity and establish it as a candidate natural scaffold for the design of isoform-selective p38 inhibitors. Full article

(This article belongs to the Special Issue Marine Glycobiology)

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18 pages, 3596 KB

Open AccessArticle

Synthesis, Biological Evaluation, and Computational Studies of Phenolic N-Acetylglucosamine Glycosides as α-Glucosidase Inhibitors

by Wenjie Wang, Kun Gao, Guantian Li, Zongji Wang, Kecheng Li, Song Liu, Huahua Yu and Ronge Xing

Mar. Drugs 2026, 24(2), 84; https://doi.org/10.3390/md24020084 - 19 Feb 2026

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Abstract

Type 2 diabetes mellitus (T2DM) is one of the most prevalent chronic metabolic diseases, and inhibition of α-glucosidase activity represents an effective therapeutic strategy. Chitin is the most abundant renewable polysaccharide in the ocean, with its monosaccharide being N-acetylglucosamine (NAG). To evaluate the potential of NAG glycosides as novel α-glucosidase inhibitors, three common phenolic compounds were modified via NAG glycosylation. Their inhibitory activities were assessed at both the enzymatic and cellular levels. In addition, density functional theory (DFT), molecular dynamics (MD) simulations, and molecular docking analyses were employed to systematically investigate the effects of NAG glycosylation on enzyme inhibition and the underlying mechanisms. Compared with the parent phenolic compounds, NAG glycosides exhibited significantly enhanced α-glucosidase inhibitory activity, with NAG introduction markedly improving their binding affinity to α-glucosidase. Among them, glycoside 3a displayed the optimal inhibitory effect, comparable to acarbose, and at the cellular level, its activity at high concentrations was comparable to or slightly higher than that of metformin. Circular dichroism (CD) and MD analyses indicated that glycoside 3a increased the conformational flexibility of key residues and enhanced the structural looseness of the enzyme, thereby inhibiting its activity. NAG glycosides constitute a promising class of marine-derived α-glucosidase inhibitors, warranting further structural optimization and rational design to enhance their activity and selectivity. Full article

(This article belongs to the Special Issue Marine Glycobiology)

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26 pages, 2533 KB

Open AccessArticle

A Sulfated Polysaccharide from Red Seaweed Gracilaria caudata Exhibits Antioxidant and Antiadipogenic Activities In Vitro

by Maxsuell Lucas Mendes Marques, Leandro Silva Costa, Mariana Santana Santos Pereira Costa and Hugo Alexandre Oliveira Rocha

Mar. Drugs 2026, 24(1), 15; https://doi.org/10.3390/md24010015 - 26 Dec 2025

Cited by 1 | Viewed by 1063

Abstract

This study investigated the antioxidant and antiadipogenic activities of sulfated polysaccharide (SPs) from the red seaweed Gracilaria caudata. First, sulfated polysaccharide-rich extracts (SPREs) from fifteen tropical seaweeds were screened to evaluate both their chemical composition and antioxidant potential. Among all samples, G. caudata exhibited the highest total antioxidant capacity, which justified its selection for detailed characterization. Sequential acetone precipitation produced three SPs (F1.5, F2.0, and F3.0), differing in sulfate content, monosaccharide composition, and molecular weight. In vitro assays revealed that F1.5 had the highest total antioxidant capacity and strong iron-chelating activity, while F2.0 exhibited the most effective hydroxyl radical scavenger. Importantly, F1.5 was the only SP that was non-cytotoxic to non-tumor cell lines. In 3T3-L1 preadipocytes, F1.5 attenuated H₂O₂-induced oxidative stress by reducing ROS and MDA levels and restoring GSH and SOD activity, achieving effects comparable to those of quercetin. Moreover, F1.5 inhibited adipogenic differentiation in a dose-dependent manner, as evidenced by decreased Oil Red O staining and reduced glycerol release. Collectively, these findings indicate that F1.5 exerts both antioxidant and antiadipogenic activities, highlighting G. caudata as a promising natural source of bioactive polysaccharides with potential nutraceutical applications. Nonetheless, further studies are required to elucidate the molecular mechanisms underlying these effects, validate the efficacy in vivo, and assess bioavailability and safety before clinical translation can be considered. Full article

(This article belongs to the Special Issue Marine Glycobiology)

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11 pages, 3264 KB

Open AccessArticle

An Oncolytic Vaccinia Virus Expressing Aphrocallistes Vastus Lectin Modulates Hepatocellular Carcinoma Metabolism via ACSS2/TFEB-Mediated Autophagy and Lipid Accumulation

by Qiang Wang, Simeng Zhou, Yin Wang, Yajun Gao, Yanrong Zhou, Ting Ye, Gongchu Li and Kan Chen

Mar. Drugs 2025, 23(8), 297; https://doi.org/10.3390/md23080297 - 24 Jul 2025

Cited by 2 | Viewed by 1729

Abstract

Hepatocellular carcinoma (HCC) remains a therapeutic challenge due to metabolic plasticity and drug resistance. Oncolytic viruses (OVs), such as thymidine kinase-deleted vaccinia virus (oncoVV), selectively lyse tumors while stimulating antitumor immunity, however, their metabolic interplay with cancer cells is poorly understood. Here, we engineered an oncoVV-expressing Aphrocallistes vastus lectin (oncoVV-AVL) and uncovered its unique ability to exploit the ACSS2/TFEB axis, driving metabolic competition in HCC. In vitro, oncoVV-AVL triggered cell autophagy and lipid accumulation (3.4–5.7-fold upregulation of FASN and ACC1) while suppressing glucose uptake (41–63% higher extracellular glucose and 33–34% reduced lactate). Mechanistically, oncoVV-AVL upregulated acetyl-CoA synthetase 2 (ACSS2), promoting its nuclear translocation and interaction with transcription factor EB (TFEB) to concurrently activate lipogenesis and autophagic flux. The pharmacological inhibition of ACSS2 abolished these effects, confirming its central role. In vivo, oncoVV-AVL suppressed tumor growth while inducing lipid deposition (2-fold triglyceride increase), systemic hypoglycemia (42% glucose reduction), and autophagy activation (elevated LC3B-II/I ratios). This study establishes ACSS2 as a metabolic checkpoint in OV therapy, providing a rationale for combining oncolytic virotherapy with metabolic modulators in HCC. Full article

(This article belongs to the Special Issue Marine Glycobiology)

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Review

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37 pages, 4829 KB

Open AccessReview

C-Type Lectins from Marine Bivalves: Functional Diversity and Structural Insights

by Ivan Buriak, Daria Lanskikh, Ivan Baklanov, Daniil Kozyrev and Andrei Grinchenko

Mar. Drugs 2026, 24(1), 17; https://doi.org/10.3390/md24010017 - 26 Dec 2025

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Abstract

C-type lectins (CTLs) are a large family of calcium-dependent carbohydrate-binding proteins that play crucial roles in innate immunity as pattern recognition receptors. Bivalve mollusks possess exceptionally diverse and expanded repertoires of CTLs, yet a systematic review integrating their structural, functional, and regulatory aspects has been lacking. This article provides a comprehensive synthesis of current knowledge on bivalve CTLs, analyzing their biosynthesis, complex tissue-specific expression under both normal and stressed conditions, and their multifaceted roles in immune defense and other physiological processes. Our analysis consolidates data on their diverse domain architectures, phylogenetic relationships, and the variability of key motifs within their carbohydrate-recognition domains. The results demonstrate that bivalve CTLs are not only critical for pathogen recognition, agglutination, and phagocytosis but also involved in processes like nutrition, development, byssus formation and biomineralization. However, a significant finding is that the detailed carbohydrate specificity for most bivalve CTLs remains poorly characterized, often limited to monosaccharide inhibition assays. In conclusion, while the immune role of bivalve CTLs is well-established, this review underscores a critical gap in understanding their fine glycan-binding profiles. Therefore, a shift in the focus of future research towards elucidating their structure and carbohydrate specificity is required for a full understanding of their biological functions and an assessment of their biomedical potential. Full article

(This article belongs to the Special Issue Marine Glycobiology)

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