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Marine Drugs
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Enzyme Inhibitor from Marine Organisms
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Enzyme Inhibitor from Marine Organisms

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

Deadline for manuscript submissions: closed (31 May 2020) | Viewed by 28072

Printed Edition Available!
A printed edition of this Special Issue is available here.

Special Issue Editor

Dr. Dirk Tischler

E-Mail Website
Guest Editor
Tech Univ Bergakad Freiberg, Inst Biosci, Environm Microbiol Grp, Freiberg, Germany.
Ruhr-University Bochum, Microbial Biotechnology Grp, Bochum, Germany.
Interests: enzyme catalysis; oxidoreductases; secondary metabolites; biotransformation; enzyme mechanism and structure
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Marine habitats are promising sources to identify novel organisms and compounds. A total of 70% of the planet’s surface is covered by oceans, and little is known about the biosphere within these habitats. In the last few years, a number of original articles and reviews have reported on the potential of identifying novel bioactive compounds or secondary metabolites from marine environments. This is, and will be, a promising source for candidate compounds in pharma research and chemical biology. As in recent years, a number of novel techniques were introduced into the field and it has become easier to actually prospect for compounds, such as enzyme inhibitors. Those novel compounds than need to be characterized and evaluated in comparison to well-known representatives. This Special Issue focuses on the description of novel enzyme inhibitors of marine origin, including bioprospecting, omic approaches, structural and mechanistic aspects.

A number of current research projects target the exploitation of marine organisms and thus the corresponding diversity of metabolites. Those are often encountered as potential drugs or biological active compounds. Among those, the class of enzyme inhibitors is an important group of compounds. There is room for new discoveries and novel inhibitors and mechanisms are frequently reported. Thus, this Special Issue aims at collecting contributions from the field and providing a platform to make them more visible to the community.

Dr. Dirk Tischler
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

  • Enzyme inhibitor
  • Protein-ligand interaction
  • Marine sponges
  • Marine bacteria
  • Secondary metabolites
  • Metabolomics
  • Chemical biology
  • Bioprospecting

Published Papers (7 papers)

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Editorial

Jump to: Research, Review

4 pages, 200 KiB  
Editorial
A Perspective on Enzyme Inhibitors from Marine Organisms
by Dirk Tischler
Mar. Drugs 2020, 18(9), 431; https://doi.org/10.3390/md18090431 - 19 Aug 2020
Cited by 7 | Viewed by 2403
Abstract
Marine habitats are promising sources for the identification of novel organisms as well as natural products. Still, we lack detailed knowledge on most of the marine biosphere. In the last decade, a number of reports described the potential of identifying novel bioactive compounds [...] Read more.
Marine habitats are promising sources for the identification of novel organisms as well as natural products. Still, we lack detailed knowledge on most of the marine biosphere. In the last decade, a number of reports described the potential of identifying novel bioactive compounds or secondary metabolites from marine environments. This is, and will be, a promising source for candidate compounds in pharma research and chemical biology. In recent years, a number of novel techniques were introduced into the field, and it has become easier to actually prospect for natural products, such as enzyme inhibitors. These novel compounds then need to be characterized and evaluated in comparison to well-known representatives. A number of current research projects target the exploitation of marine organisms and thus the corresponding diversity of metabolites. These are often encountered as potential drugs or biological active compounds. Among these, the class of enzyme inhibitors is an important group of compounds. There is room for new discoveries, and some more recent discoveries are highlighted herein. Full article
(This article belongs to the Special Issue Enzyme Inhibitor from Marine Organisms)

Research

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15 pages, 2795 KiB  
Article
Partial Characterization of Protease Inhibitors of Ulva ohnoi and Their Effect on Digestive Proteases of Marine Fish
by Antonio Jesús Vizcaíno, Alba Galafat, María Isabel Sáez, Tomás Francisco Martínez and Francisco Javier Alarcón
Mar. Drugs 2020, 18(6), 319; https://doi.org/10.3390/md18060319 - 18 Jun 2020
Cited by 13 | Viewed by 3111
Abstract
This piece of research evaluates the presence of protease inhibitors in the macroalga Ulva ohnoi and provides an initial overview of their mode of action. The ability of Ulva protease inhibitors to inhibit digestive proteases of three marine fish species, as well as [...] Read more.
This piece of research evaluates the presence of protease inhibitors in the macroalga Ulva ohnoi and provides an initial overview of their mode of action. The ability of Ulva protease inhibitors to inhibit digestive proteases of three marine fish species, as well as their capacity to hamper the hydrolysis of a reference protein by those fish proteases, were assessed. In addition, thermal stability and the mode of inhibition on trypsin and chymotrypsin were also studied. Dose-response inhibition curves and in vitro protein hydrolysis assays revealed a noticeable inhibition of fish enzymes when Ulva concentration increased in the assay. The thermal treatment of Ulva reduced markedly the inhibitory effect on fish digestive protease. Finally, Lineweaver–Burk plots indicated that trypsin and chymotrypsin inhibition consisted of a mixed-type inhibition mechanism in which the inhibitory effect depends on Ulva concentration. Overall, the results confirmed the presence of protease inhibitors in Ulva, though heat treatment was enough for inactivating these compounds. Full article
(This article belongs to the Special Issue Enzyme Inhibitor from Marine Organisms)
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11 pages, 1097 KiB  
Article
Secondary Metabolites with α-Glucosidase Inhibitory Activity from the Mangrove Fungus Mycosphaerella sp. SYSU-DZG01
by Pei Qiu, Zhaoming Liu, Yan Chen, Runlin Cai, Guangying Chen and Zhigang She
Mar. Drugs 2019, 17(8), 483; https://doi.org/10.3390/md17080483 - 20 Aug 2019
Cited by 17 | Viewed by 3403
Abstract
Four new metabolites, asperchalasine I (1), dibefurin B (2) and two epicoccine derivatives (3 and 4), together with seven known compounds (5–11) were isolated from a mangrove fungus Mycosphaerella sp. SYSU-DZG01. The structures [...] Read more.
Four new metabolites, asperchalasine I (1), dibefurin B (2) and two epicoccine derivatives (3 and 4), together with seven known compounds (5–11) were isolated from a mangrove fungus Mycosphaerella sp. SYSU-DZG01. The structures of compounds 1–4 were established from extensive spectroscopic data and HRESIMS analysis. The absolute configuration of 1 was deduced by comparison of ECD data with that of a known structure. The stereostructures of 2–4 were further confirmed by single-crystal X-ray diffraction. Compounds 1, 8 and 9 exhibited significant α-glucosidase inhibitory activity with IC50 values of 17.1, 26.7 and 15.7 μM, respectively. Compounds 1, 4, 6 and 8 showed antioxidant activity by scavenging DPPH· with EC50 values ranging from 16.3 to 85.8 μM. Full article
(This article belongs to the Special Issue Enzyme Inhibitor from Marine Organisms)
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17 pages, 3620 KiB  
Article
Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis
by Siqi Sun, Xiaoting Xu, Xue Sun, Xiaoqian Zhang, Xinping Chen and Nianjun Xu
Mar. Drugs 2019, 17(3), 179; https://doi.org/10.3390/md17030179 - 19 Mar 2019
Cited by 88 | Viewed by 5399
Abstract
Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from seaweed represent a potential source of new antihypertensive. The aim of this study was to isolate and purify ACE inhibitory peptides (ACEIPs) from the protein hydrolysate of the marine macroalga Ulva intestinalis. U. intestinalis [...] Read more.
Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from seaweed represent a potential source of new antihypertensive. The aim of this study was to isolate and purify ACE inhibitory peptides (ACEIPs) from the protein hydrolysate of the marine macroalga Ulva intestinalis. U. intestinalis protein was hydrolyzed by five different proteases (trypsin, pepsin, papain, α-chymotrypsin, alcalase) to prepare peptides; compared with other hydrolysates, the trypsin hydrolysates exhibited the highest ACE inhibitory activity. The hydrolysis conditions were further optimized by response surface methodology (RSM), and the optimum conditions were as follows: pH 8.4, temperature 28.5 °C, enzyme/protein ratio (E/S) 4.0%, substrate concentration 15 mg/mL, and enzymolysis time 5.0 h. After fractionation and purification by ultrafiltration, gel exclusion chromatography and reverse-phase high-performance liquid chromatography, two novel purified ACE inhibitors with IC50 values of 219.35 μM (0.183 mg/mL) and 236.85 μM (0.179 mg/mL) were obtained. The molecular mass and amino acid sequence of the ACE inhibitory peptides were identified as Phe-Gly-Met-Pro-Leu-Asp-Arg (FGMPLDR; MW 834.41 Da) and Met-Glu-Leu-Val-Leu-Arg (MELVLR; MW 759.43 Da) by ultra-performance liquid chromatography-tandem mass spectrometry. A molecular docking study revealed that the ACE inhibitory activities of the peptides were mainly attributable to the hydrogen bond and Zn(II) interactions between the peptides and ACE. The results of this study provide a theoretical basis for the high-valued application of U. intestinalis and the development of food-derived ACE inhibitory peptides. Full article
(This article belongs to the Special Issue Enzyme Inhibitor from Marine Organisms)
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15 pages, 2688 KiB  
Article
Dual BACE1 and Cholinesterase Inhibitory Effects of Phlorotannins from Ecklonia cava—An In Vitro and in Silico Study
by Jinhyuk Lee and Mira Jun
Mar. Drugs 2019, 17(2), 91; https://doi.org/10.3390/md17020091 - 01 Feb 2019
Cited by 41 | Viewed by 3469
Abstract
Alzheimer′s disease (AD) is one of the most common neurodegenerative diseases with a multifactorial nature. β-Secretase (BACE1) and acetylcholinesterase (AChE), which are required for the production of neurotoxic β-amyloid (Aβ) and the promotion of Aβ fibril formation, respectively, are considered as prime therapeutic [...] Read more.
Alzheimer′s disease (AD) is one of the most common neurodegenerative diseases with a multifactorial nature. β-Secretase (BACE1) and acetylcholinesterase (AChE), which are required for the production of neurotoxic β-amyloid (Aβ) and the promotion of Aβ fibril formation, respectively, are considered as prime therapeutic targets for AD. In our efforts towards the development of potent multi-target, directed agents for AD treatment, major phlorotannins such as eckol, dieckol, and 8,8′-bieckol from Ecklonia cava (E. cava) were evaluated. Based on the in vitro study, all tested compounds showed potent inhibitory effects on BACE1 and AChE. In particular, 8,8′-bieckol demonstrated the best inhibitory effect against BACE1 and AChE, with IC50 values of 1.62 ± 0.14 and 4.59 ± 0.32 µM, respectively. Overall, kinetic studies demonstrated that all the tested compounds acted as dual BACE1 and AChE inhibitors in a non-competitive or competitive fashion, respectively. In silico docking analysis exhibited that the lowest binding energies of all compounds were negative, and specifically different residues of each target enzyme interacted with hydroxyl groups of phlorotannins. The present study suggested that major phlorotannins derived from E. cava possess significant potential as drug candidates for therapeutic agents against AD. Full article
(This article belongs to the Special Issue Enzyme Inhibitor from Marine Organisms)
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15 pages, 2063 KiB  
Article
Effect of Pentacyclic Guanidine Alkaloids from the Sponge Monanchora pulchra on Activity of α-Glycosidases from Marine Bacteria
by Irina Bakunina, Galina Likhatskaya, Lubov Slepchenko, Larissa Balabanova, Liudmila Tekutyeva, Oksana Son, Larisa Shubina and Tatyana Makarieva
Mar. Drugs 2019, 17(1), 22; https://doi.org/10.3390/md17010022 - 01 Jan 2019
Cited by 9 | Viewed by 3048
Abstract
The effect of monanchomycalin B, monanhocicidin A, and normonanhocidin A isolated from the Northwest Pacific sample of the sponge Monanchora pulchra was investigated on the activity of α-galactosidase from the marine γ-proteobacterium Pseudoalteromonas sp. KMM 701 (α-PsGal), and α-N-acetylgalactosaminidase from the [...] Read more.
The effect of monanchomycalin B, monanhocicidin A, and normonanhocidin A isolated from the Northwest Pacific sample of the sponge Monanchora pulchra was investigated on the activity of α-galactosidase from the marine γ-proteobacterium Pseudoalteromonas sp. KMM 701 (α-PsGal), and α-N-acetylgalactosaminidase from the marine bacterium Arenibacter latericius KMM 426T (α-NaGa). All compounds are slow-binding irreversible inhibitors of α-PsGal, but have no effect on α-NaGa. A competitive inhibitor d-galactose protects α-PsGal against the inactivation. The inactivation rate (kinact) and equilibrium inhibition (Ki) constants of monanchomycalin B, monanchocidin A, and normonanchocidin A were 0.166 ± 0.029 min−1 and 7.70 ± 0.62 μM, 0.08 ± 0.003 min−1 and 15.08 ± 1.60 μM, 0.026 ± 0.000 min−1, and 4.15 ± 0.01 μM, respectively. The 2D-diagrams of α-PsGal complexes with the guanidine alkaloids were constructed with “vessel” and “anchor” parts of the compounds. Two alkaloid binding sites on the molecule of α-PsGal are shown. Carboxyl groups of the catalytic residues Asp451 and Asp516 of the α-PsGal active site interact with amino groups of “anchor” parts of the guanidine alkaloid molecules. Full article
(This article belongs to the Special Issue Enzyme Inhibitor from Marine Organisms)
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Review

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37 pages, 11579 KiB  
Review
A Systematic Review of Recently Reported Marine Derived Natural Product Kinase Inhibitors
by Te Li, Ning Wang, Ting Zhang, Bin Zhang, Thavarool P. Sajeevan, Valsamma Joseph, Lorene Armstrong, Shan He, Xiaojun Yan and C. Benjamin Naman
Mar. Drugs 2019, 17(9), 493; https://doi.org/10.3390/md17090493 - 23 Aug 2019
Cited by 35 | Viewed by 6311
Abstract
Protein kinases are validated drug targets for a number of therapeutic areas, as kinase deregulation is known to play an essential role in many disease states. Many investigated protein kinase inhibitors are natural product small molecules or their derivatives. Many marine-derived natural products [...] Read more.
Protein kinases are validated drug targets for a number of therapeutic areas, as kinase deregulation is known to play an essential role in many disease states. Many investigated protein kinase inhibitors are natural product small molecules or their derivatives. Many marine-derived natural products from various marine sources, such as bacteria and cyanobacteria, fungi, animals, algae, soft corals, sponges, etc. have been found to have potent kinase inhibitory activity, or desirable pharmacophores for further development. This review covers the new compounds reported from the beginning of 2014 through the middle of 2019 as having been isolated from marine organisms and having potential therapeutic applications due to kinase inhibitory and associated bioactivities. Moreover, some existing clinical drugs based on marine-derived natural product scaffolds are also discussed. Full article
(This article belongs to the Special Issue Enzyme Inhibitor from Marine Organisms)
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