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Bioactive Natural Products: Isolation, Structural Elucidation and Biological Assays, 2nd Edition

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Bioactives and Nutraceuticals".

Deadline for manuscript submissions: closed (30 August 2024) | Viewed by 3798

Special Issue Editor

Prof. Dr. Antonio Evidente

E-Mail Website
Guest Editor
Institute of Biomolecular Chemistry, National Research Council, Via Campi Flegrei 34, 80078 Pozzuoli, Italy
Interests: natural bioactive substances; spectroscopy; isolation; structure determination; structure–activity relationships; mode of action
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue is the continuation of our Special Issue https://www.mdpi.com/journal/ijms/special_issues/Bioactive_
Structural.

The natural sources had been always important to find new compounds with different chemical structure and biological activity with potential practical application in different fields. The source is essentially constituted by terrestrial and marine organisms and microorganism, and among them pathogen or endophytic fungi, bacteria, plant and marine organisms. Lichens, although lesser investigated, also are considered a source for natural compounds with original skeleton and biological activity. Thus the main aims of the special volume are the isolation and chemical and biological characterization of microbial, plant and lichen metabolites. Also article describing their derivatization for structure-activity relationships or mode of action studies and BIOFORMULATION are welcome. The results of mutidiciplinary research projects are preferred. The manuscript could be a scientific work or a reviewer.

Prof. Dr. Antonio Evidente
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • natural compounds
  • chemical characterization
  • biological charaterization
  • derivatization
  • structure-activity relationships
  • mode of action
  • bioformulation

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Published Papers (2 papers)

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Research

13 pages, 1608 KiB  
Article
Assessing the Efficacy of Protease Inactivation for the Preservation of Bioactive Amphibian Skin Peptides
by Tatiana Yu. Samgina, Dmitrii M. Mazur and Albert T. Lebedev
Int. J. Mol. Sci. 2024, 25(16), 8759; https://doi.org/10.3390/ijms25168759 - 12 Aug 2024
Cited by 2 | Viewed by 1197
Abstract
The skin of amphibians is a rich source of peptides with a wide range of biological activities. They are stored in secretory granules in an inactive form. Upon stimulation, they are secreted together with proteases into the skin. Once activated, they rapidly exert [...] Read more.
The skin of amphibians is a rich source of peptides with a wide range of biological activities. They are stored in secretory granules in an inactive form. Upon stimulation, they are secreted together with proteases into the skin. Once activated, they rapidly exert their biological effects, including fighting microorganisms and predators, while their excess is immediately destroyed by the released proteases. To keep bioactive peptides in their initial form, it is necessary to inhibit these enzymes. Several inhibitors for this purpose have previously been mentioned; however, there has not been any reliable comparison of their efficiency so far. Here, we studied the efficiency of methanol and hydrochloric and formic acids, as well as phenylmethylsulfonyl fluoride, in the inhibition of nine frog peptides with the known sequence, belonging to five families in the secretion of Pelophylax esculentus. The results demonstrated that methanol had the highest inhibitory efficiency, while phenylmethylsulfonyl fluoride was the least efficient, probably due to its instability in aqueous media. Possible cleavages between certain amino acid residues in the sequence were established for each of the inhibitors. These results may be helpful for future studies on the nature of proteases and on prediction of the possible cleavage sites in novel peptides. Full article
(This article belongs to the Special Issue Bioactive Natural Products: Isolation, Structural Elucidation and Biological Assays, 2nd Edition)
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17 pages, 2111 KiB  
Article
Madurastatins with Imidazolidinone Rings: Natural Products or Side-Reaction Products from Extraction Solvents?
by Mercedes Pérez-Bonilla, Marina Sánchez-Hidalgo, Ignacio González, Daniel Oves-Costales, Jesús Martín, José Murillo-Alba, José R. Tormo, Ahreum Cho, Soo-Young Byun, Joo-Hwan No, David Shum, Jean-Robert Ioset, Olga Genilloud and Fernando Reyes
Int. J. Mol. Sci. 2024, 25(1), 301; https://doi.org/10.3390/ijms25010301 - 25 Dec 2023
Cited by 1 | Viewed by 1891
Abstract
Madurastatins are a group of pentapeptides containing an oxazoline moiety, and, in a few cases, an imidazolidinone ring as an additional structural feature. In our search for new potential antiparasitic metabolites from natural sources, we studied the acetone extracts from a culture of [...] Read more.
Madurastatins are a group of pentapeptides containing an oxazoline moiety, and, in a few cases, an imidazolidinone ring as an additional structural feature. In our search for new potential antiparasitic metabolites from natural sources, we studied the acetone extracts from a culture of Actinomadura sp. CA-135719. The LC/HRMS analysis of this extract identified the presence of the known madurastatins C1 (1), D1 (4), and D2 (5) together with additional members of the family that were identified as the new madurastatins H2 (2) and 33-epi-D1 (3) after isolation and spectroscopic analysis. The planar structures of the new compounds were established by HRMS, ESI-qTOF-MS/MS, and 1D and 2D NMR data, and their absolute configuration was proposed using Marfey’s and bioinformatic analyses of the biosynthetic gene cluster (BGC). A revision of the absolute configuration of madurastatins D1 and D2 is proposed. Additionally, madurastatins containing imidazolidinone rings are proved to be artifacts originating during acetone extraction of the bacterial cultures. Full article
(This article belongs to the Special Issue Bioactive Natural Products: Isolation, Structural Elucidation and Biological Assays, 2nd Edition)
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