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Special Issue "Enzyme Inhibitors of Marine Origin"

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

Deadline for manuscript submissions: closed (28 February 2017)

Special Issue Editor

Guest Editor
Prof. Dr. Sadanandan E. Velu

Department of Chemistry, CHEM-280, The University of Alabama at Birmingham 901, 14th Street South, Birmingham, AL 35294-1240, USA
Website | E-Mail
Phone: (205) 975 2478
Fax: +1 205 934 2543
Interests: bioactive marine alkaloids; analogues; synthesis; anti-cancer; anti-infective; enzyme inhibitors; structure based drug design; fragment based drug design; in silico virtual screening; SAR studies; lead optimization

Special Issue Information

Dear Colleagues,

Marine natural products have recently received increased attention as a source of lead compounds for drug discovery. These compounds are initially identified based on bioactivity screens and their mode of action is largely unknown. Discerning their mode of action is a critical step in their further development as potential drugs. Many of such lead compounds are enzyme inhibitors. This Special Issue focuses on such marine-derived natural products or their analogs that are enzyme inhibitors. The coverage includes the biological activities of the lead compounds, identification of the target enzyme, location of the enzyme binding site and the mechanistic details of the enzyme inhibition. We aim to publish both original research articles and review articles in this Special Issue.

Prof. Dr. Sadanandan E. Velu
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 papers will be 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 1800 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 alkaloid
  • analog
  • synthesis
  • cytotoxic
  • anticancer
  • anti-inflammatory
  • antibacterial
  • antimalarial
  • antiviral
  • enzyme inhibitor
  • non-specific
  • specific
  • irreversible
  • reversible
  • competitive
  • non-competitive
  • allosteric

Published Papers (5 papers)

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Research

Open AccessArticle Identification of Tight-Binding Plasmepsin II and Falcipain 2 Inhibitors in Aqueous Extracts of Marine Invertebrates by the Combination of Enzymatic and Interaction-Based Assays
Mar. Drugs 2017, 15(4), 123; doi:10.3390/md15040123
Received: 28 February 2017 / Revised: 16 April 2017 / Accepted: 18 April 2017 / Published: 21 April 2017
PDF Full-text (5474 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Natural products from marine origin constitute a very promising and underexplored source of interesting compounds for modern biotechnological and pharmaceutical industries. However, their evaluation is quite challenging and requires specifically designed assays to reliably identify the compounds of interest in a highly heterogeneous
[...] Read more.
Natural products from marine origin constitute a very promising and underexplored source of interesting compounds for modern biotechnological and pharmaceutical industries. However, their evaluation is quite challenging and requires specifically designed assays to reliably identify the compounds of interest in a highly heterogeneous and interfering context. In the present study, we describe a general strategy for the confident identification of tight-binding protease inhibitors in the aqueous extracts of 62 Cuban marine invertebrates, using Plasmodium falciparum hemoglobinases Plasmepsin II and Falcipain 2 as model enzymes. To this end, we first developed a screening strategy that combined enzymatic with interaction-based assays and then validated screening conditions using five reference extracts. Interferences were evaluated and minimized. The results from the massive screening of such extracts, the validation of several hits by a variety of interaction-based assays and the purification and functional characterization of PhPI, a multifunctional and reversible tight-binding inhibitor for Plasmepsin II and Falcipain 2 from the gorgonian Plexaura homomalla, are presented. Full article
(This article belongs to the Special Issue Enzyme Inhibitors of Marine Origin)
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Open AccessArticle Optimization of Bromelain-Aided Production of Angiotensin I-Converting Enzyme Inhibitory Hydrolysates from Stone Fish Using Response Surface Methodology
Mar. Drugs 2017, 15(4), 104; doi:10.3390/md15040104
Received: 8 November 2016 / Revised: 15 March 2017 / Accepted: 24 March 2017 / Published: 31 March 2017
Cited by 2 | PDF Full-text (1840 KB) | HTML Full-text | XML Full-text
Abstract
The stone fish is an under-utilized sea cucumber with many nutritional and ethno-medicinal values. This study aimed to establish the conditions for its optimum hydrolysis with bromelain to generate angiotensin I-converting enzyme (ACE)-inhibitory hydrolysates. Response surface methodology (RSM) based on a central composite
[...] Read more.
The stone fish is an under-utilized sea cucumber with many nutritional and ethno-medicinal values. This study aimed to establish the conditions for its optimum hydrolysis with bromelain to generate angiotensin I-converting enzyme (ACE)-inhibitory hydrolysates. Response surface methodology (RSM) based on a central composite design was used to model and optimize the degree of hydrolysis (DH) and ACE-inhibitory activity. Process conditions including pH (4–7), temperature (40–70 °C), enzyme/substrate (E/S) ratio (0.5%–2%) and time (30–360 min) were used. A pH of 7.0, temperature of 40 °C, E/S ratio of 2% and time of 240 min were determined using a response surface model as the optimum levels to obtain the maximum ACE-inhibitory activity of 84.26% at 44.59% degree of hydrolysis. Hence, RSM can serve as an effective approach in the design of experiments to improve the antihypertensive effect of stone fish hydrolysates, which can thus be used as a value-added ingredient for various applications in the functional foods industries. Full article
(This article belongs to the Special Issue Enzyme Inhibitors of Marine Origin)
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Figure 1a

Open AccessArticle New Enzyme-Inhibitory Triterpenoid from Marine Macro Brown Alga Padina boergesenii Allender & Kraft
Mar. Drugs 2017, 15(1), 19; doi:10.3390/md15010019
Received: 3 November 2016 / Revised: 27 December 2016 / Accepted: 27 December 2016 / Published: 18 January 2017
PDF Full-text (1077 KB) | HTML Full-text | XML Full-text
Abstract
In continuation to our study of the chemical and biological potential of the secondary metabolites isolated from Omani seaweeds, we investigated a marine brown alga, Padina boergesenii. The phytochemical investigation resulted in the isolation of a new secondary metabolite, padinolic acid (
[...] Read more.
In continuation to our study of the chemical and biological potential of the secondary metabolites isolated from Omani seaweeds, we investigated a marine brown alga, Padina boergesenii. The phytochemical investigation resulted in the isolation of a new secondary metabolite, padinolic acid (1), along with some other semi-pure fractions and sub-fractions. The planar structure was confirmed through MS and NMR (1D and 2D) spectral data. The NOESY experiments coupled with the biogenetic consideration were helpful in assigning the stereochemistry in the molecule. Compound 1 was subjected to enzyme inhibition studies using urease, lipid peroxidase, and alpha-glucosidase enzymes. Compound 1 showed low to moderate α-glucosidase and urease enzyme inhibition, respectively, and moderate anti-lipid peroxidation activities. The current study indicates the potential of this seaweed and provides the basis for further investigation. Full article
(This article belongs to the Special Issue Enzyme Inhibitors of Marine Origin)
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Figure 1

Open AccessArticle Natural Products from Microalgae with Potential against Alzheimer’s Disease: Sulfolipids Are Potent Glutaminyl Cyclase Inhibitors
Mar. Drugs 2016, 14(11), 203; doi:10.3390/md14110203
Received: 16 September 2016 / Revised: 20 October 2016 / Accepted: 25 October 2016 / Published: 2 November 2016
Cited by 3 | PDF Full-text (1067 KB) | HTML Full-text | XML Full-text
Abstract
In recent years, many new enzymes, like glutaminyl cyclase (QC), could be associated with pathophysiological processes and represent targets for many diseases, so that enzyme-inhibiting properties of natural substances are becoming increasingly important. In different studies, the pathophysiology connection of QC to various
[...] Read more.
In recent years, many new enzymes, like glutaminyl cyclase (QC), could be associated with pathophysiological processes and represent targets for many diseases, so that enzyme-inhibiting properties of natural substances are becoming increasingly important. In different studies, the pathophysiology connection of QC to various diseases including Alzheimer’s disease (AD) was described. Algae are known for the ability to synthesize complex and highly-diverse compounds with specific enzyme inhibition properties. Therefore, we screened different algae species for the presence of QC inhibiting metabolites using a new “Reverse Metabolomics” technique including an Activity-correlation Analysis (AcorA), which is based on the correlation of bioactivities to mass spectral data with the aid of mathematic informatics deconvolution. Thus, three QC inhibiting compounds from microalgae belonging to the family of sulfolipids were identified. The compounds showed a QC inhibition of 81% and 76% at concentrations of 0.25 mg/mL and 0.025 mg/mL, respectively. Thus, for the first time, sulfolipids are identified as QC inhibiting compounds and possess substructures with the required pharmacophore qualities. They represent a new lead structure for QC inhibitors. Full article
(This article belongs to the Special Issue Enzyme Inhibitors of Marine Origin)
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Figure 1

Open AccessArticle Different Culture Metabolites of the Red Sea Fungus Fusarium equiseti Optimize the Inhibition of Hepatitis C Virus NS3/4A Protease (HCV PR)
Mar. Drugs 2016, 14(10), 190; doi:10.3390/md14100190
Received: 30 August 2016 / Revised: 29 September 2016 / Accepted: 11 October 2016 / Published: 20 October 2016
PDF Full-text (1034 KB) | HTML Full-text | XML Full-text
Abstract
The endophytic fungus Fusarium equiseti was isolated from the brown alga Padina pavonica, collected from the Red Sea. The fungus was identified by its morphology and 18S rDNA. Cultivation of this fungal strain in biomalt-peptone medium led to isolation of 12 known
[...] Read more.
The endophytic fungus Fusarium equiseti was isolated from the brown alga Padina pavonica, collected from the Red Sea. The fungus was identified by its morphology and 18S rDNA. Cultivation of this fungal strain in biomalt-peptone medium led to isolation of 12 known metabolites of diketopeprazines and anthraquinones. The organic extract and isolated compounds were screened for their inhibition of hepatitis C virus NS3/4A protease (HCV PR). As a result, the fungal metabolites showed inhibition of HCV protease (IC50 from 19 to 77 μM), and the fungus was subjected to culture on Czapek’s (Cz) media, with a yield of nine metabolites with potent HCV protease inhibition ranging from IC50 10 to 37 μM. The Cz culture extract exhibited high-level inhibition of HCV protease (IC50 27.6 μg/mL) compared to the biomalt culture extract (IC50 56 μg/mL), and the most potent HCV PR isolated compound (Griseoxanthone C, IC50 19.8 μM) from the bio-malt culture extract showed less of an inhibitory effect compared to isolated ω-hydroxyemodin (IC50 10.7 μM) from the optimized Cz culture extract. Both HCV PR active inhibitors ω-hydroxyemodin and griseoxanthone C were considered as the lowest selective safe constituents against Trypsin inhibitory effect with IC50 48.5 and 51.3 μM, respectively. Full article
(This article belongs to the Special Issue Enzyme Inhibitors of Marine Origin)
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Figure 1a

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