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Marine Drugs
Special Issues
Biosynthesis of Biologically Active Marine Natural Products 2025
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Biosynthesis of Biologically Active Marine Natural Products 2025

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

Deadline for manuscript submissions: 15 June 2025 | Viewed by 1195

Special Issue Editor

Prof. Dr. Yiguang Zhu

E-Mail Website
Guest Editor
South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou 510301, China
Interests: marine actinomycetes; marine fungi; marine natural products; biosynthetic pathway; enzymatic reaction mechanisms

Special Issue Information

Dear Colleagues,

The marine environment, with its vast biodiversity, is home to a plethora of organisms that are capable of producing a wide array of bioactive natural products. Marine organisms, including bacteria, fungi, algae, corals, and sponges, have evolved to produce these specialized compounds as part of their natural defense mechanisms or ecological interactions. These bioactive molecules represent a rich and diverse source of chemical entities with remarkable pharmacological potential. Marine natural products have attracted enhanced attention in recent years due to their unique chemical structures, novel modes of action, and considerable promise as candidates for drug discovery and development.

This Special Issue will focus on the biosynthesis of marine natural products, exploring the complex biochemical pathways through which these compounds are synthesized in marine organisms. This Special Issue aims to highlight the enzymes, genetic clusters, and regulatory networks that are responsible for the production of these bioactive molecules, and to explore how these biosynthetic processes can be harnessed to advance the discovery and production of new lead compounds. Additionally, this Special Issue will emphasize the extraction, isolation, structural elucidation and biological activities of marine natural products. We will particularly focus on the therapeutic potential of these compounds in treating complex diseases, including cancer, antimicrobial, and neurodegenerative diseases; this will emphasize the ability of marine-derived bioactive molecules to address medical needs.

We invite both academic and industry researchers to submit original research and review articles that investigate the biosynthetic pathways of marine natural products and their diverse biological activities. We encourage the submission of studies that bridge the gap between basic biosynthetic research and translational applications, particularly in addressing the therapeutic potential of these compounds in treating complex diseases.

Prof. Dr. Yiguang Zhu
Dr. Junfeng Wang
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 microorganisms
  • marine plants and animals
  • genome mining
  • biosynthetic pathway enzymatic reaction mechanisms
  • marine bioactive compounds
  • structure elucidation
  • bioactivity screening
  • structure–activity relationship
  • pharmacological mechanism

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

Published Papers (2 papers)

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13 pages, 1859 KiB  
Article
The Isolation, Structural Characterization, and Biosynthetic Pathway of Unguisin from the Marine-Derived Fungus Aspergillus candidus
by Wenjiao Diao, Wei Zhang, Xiaoxi Zhang, Siyu Du, Caijuan Zheng, Xuenian Huang and Xuefeng Lu
Mar. Drugs 2025, 23(5), 219; https://doi.org/10.3390/md23050219 - 21 May 2025
Viewed by 294
Abstract
Unguisins, a class of structurally complex cyclic peptides featuring a γ-aminobutyric acid residue embedded in the skeleton, exhibit diverse biological activities. Here, a new unguisin K, along with three known congeners, was isolated from the marine-derived fungus Aspergillus candidus MEFC1001. The biosynthetic [...] Read more.
Unguisins, a class of structurally complex cyclic peptides featuring a γ-aminobutyric acid residue embedded in the skeleton, exhibit diverse biological activities. Here, a new unguisin K, along with three known congeners, was isolated from the marine-derived fungus Aspergillus candidus MEFC1001. The biosynthetic pathway was elucidated through gene disruption coupled with in vitro enzymatic characterization. The ugs biosynthetic gene cluster (BGC) containing ugsA and ugsB, in conjunction with an extra-clustered gene ugsC, collaborates to synthesize these unguisins. The alanine racemase (AR) UgsC catalyzes the isomerization of Ala and provides d-Ala as the starter unit for the non-ribosomal peptide synthetase (NRPS). The unique localization of ugsC outside the ugs BGC is different from previously reported unguisin-producing systems where AR genes reside within BGCs. The methyltransferase UgsB mediates a key pre-modification step by methylating phenylpyruvic acid to yield β-methylphenylpyruvate, which is subsequently incorporated as β-methylphenylalanine during NRPS assembly. This represents the first experimental evidence of the β-carbon methylation of Phe residue occurring at the precursor level rather than through post-assembly modification. The NRPS UgsA recruits a variety of amino acids for assembly and cyclization to form mature unguisins. Additionally, genome mining utilizing UgsA as a query identified homologous NRPSs in diverse fungal species, highlighting the potential for unguisin production in fungi. This study enriches the biosynthetic diversity of cyclic peptides and provides guidance for exploring unguisin-like natural products derived from fungi. Full article
(This article belongs to the Special Issue Biosynthesis of Biologically Active Marine Natural Products 2025)
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Other

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11 pages, 991 KiB  
Perspective
The Enigma of Sponge-Derived Terpenoid Isothiocyanate–Thiocyanate Pairs: A Biosynthetic Proposal
by Tadeusz F. Molinski
Mar. Drugs 2025, 23(5), 220; https://doi.org/10.3390/md23050220 - 21 May 2025
Viewed by 202
Abstract
The co-occurrence of rare terpenoid thiocyanates (R-SCN), structurally similar to their more common isothiocyanate isomers (R-NCS), poses an enigma: how does the accepted path, terpenyl cation R+ → R-NC → R-NCS, accommodate R-SCN? The mystery can now be rationalized by the consideration [...] Read more.
The co-occurrence of rare terpenoid thiocyanates (R-SCN), structurally similar to their more common isothiocyanate isomers (R-NCS), poses an enigma: how does the accepted path, terpenyl cation R+ → R-NC → R-NCS, accommodate R-SCN? The mystery can now be rationalized by the consideration of three biosynthetic motifs: terpenoid carbocation (R+) capture by cyanoformate, NC-COOH (itself in equilibrium with NC− and CO2); co-localized rhodanese (a dual-function enzyme) that can both convert fugitive inorganic NC− to thiocyanate ion, NCS−, and alkyl isonitriles to alkyl isothiocyanate (R-NC → R-NCS) and adventitious capture of the NCS− by R+. The former two scenarios explain the preponderance of isothiocyanates, R-NCS, as products of a linear reaction path—the α-addition of S0 to R-NC—and the third scenario explains minor, less stable thiocyanates, R-SCN, as products of the adventitious capture of liberated NCS− by the penultimate R+ precursor. DFT calculations support this proposal and eliminate other possibilities, e.g., the isomerization of R-NCS to R-SCN. Full article
(This article belongs to the Special Issue Biosynthesis of Biologically Active Marine Natural Products 2025)
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