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Bioprospecting of Sea Anemones (Cnidaria, Anthozoa, Actiniaria) for β-Defensin-like α-Amylase Inhibitors

Diabetes mellitus is one of the most serious diseases of our century. The drugs used are limited or have serious side effects. The search for new sources of compounds for effective treatment is relevant. Magnificamide, a peptide inhibitor of mammalian α-amylases, isolated from the venom of sea anemo...

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Autores principales: Popkova, Daria, Otstavnykh, Nadezhda, Sintsova, Oksana, Baldaev, Sergey, Kalina, Rimma, Gladkikh, Irina, Isaeva, Marina, Leychenko, Elena
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10604346/
https://www.ncbi.nlm.nih.gov/pubmed/37893056
http://dx.doi.org/10.3390/biomedicines11102682
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author Popkova, Daria
Otstavnykh, Nadezhda
Sintsova, Oksana
Baldaev, Sergey
Kalina, Rimma
Gladkikh, Irina
Isaeva, Marina
Leychenko, Elena
author_facet Popkova, Daria
Otstavnykh, Nadezhda
Sintsova, Oksana
Baldaev, Sergey
Kalina, Rimma
Gladkikh, Irina
Isaeva, Marina
Leychenko, Elena
author_sort Popkova, Daria
collection PubMed
description Diabetes mellitus is one of the most serious diseases of our century. The drugs used are limited or have serious side effects. The search for new sources of compounds for effective treatment is relevant. Magnificamide, a peptide inhibitor of mammalian α-amylases, isolated from the venom of sea anemone Heteractis magnifica, can be used for the control of postprandial hyperglycemia in diabetes mellitus. Using the RACE approach, seven isoforms of magnificamide were detected in H. magnifica tentacles. The exon–intron structure of magnificamide genes was first established, and intron retention in the mature peptide-encoding region was revealed. Additionally, an α-amylase inhibitory domain was discovered in the mucins of some sea anemones. According to phylogenetics, sea anemones diverge into two groups depending on the presence of β-defensin-like α-amylase inhibitors and/or mucin-inhibitory domains. It is assumed that the intron retention phenomenon leads to additional diversity in the isoforms of inhibitors and allows for its neofunctionalization in sea anemone tentacles. Bioprospecting of sea anemones of the order Actiniaria for β-defensin-like α-amylase inhibitors revealed a diversity of inhibitory sequences that represents a starting point for the design of effective glucose-lowering drugs.
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spelling pubmed-106043462023-10-28 Bioprospecting of Sea Anemones (Cnidaria, Anthozoa, Actiniaria) for β-Defensin-like α-Amylase Inhibitors Popkova, Daria Otstavnykh, Nadezhda Sintsova, Oksana Baldaev, Sergey Kalina, Rimma Gladkikh, Irina Isaeva, Marina Leychenko, Elena Biomedicines Article Diabetes mellitus is one of the most serious diseases of our century. The drugs used are limited or have serious side effects. The search for new sources of compounds for effective treatment is relevant. Magnificamide, a peptide inhibitor of mammalian α-amylases, isolated from the venom of sea anemone Heteractis magnifica, can be used for the control of postprandial hyperglycemia in diabetes mellitus. Using the RACE approach, seven isoforms of magnificamide were detected in H. magnifica tentacles. The exon–intron structure of magnificamide genes was first established, and intron retention in the mature peptide-encoding region was revealed. Additionally, an α-amylase inhibitory domain was discovered in the mucins of some sea anemones. According to phylogenetics, sea anemones diverge into two groups depending on the presence of β-defensin-like α-amylase inhibitors and/or mucin-inhibitory domains. It is assumed that the intron retention phenomenon leads to additional diversity in the isoforms of inhibitors and allows for its neofunctionalization in sea anemone tentacles. Bioprospecting of sea anemones of the order Actiniaria for β-defensin-like α-amylase inhibitors revealed a diversity of inhibitory sequences that represents a starting point for the design of effective glucose-lowering drugs. MDPI 2023-09-30 /pmc/articles/PMC10604346/ /pubmed/37893056 http://dx.doi.org/10.3390/biomedicines11102682 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Popkova, Daria
Otstavnykh, Nadezhda
Sintsova, Oksana
Baldaev, Sergey
Kalina, Rimma
Gladkikh, Irina
Isaeva, Marina
Leychenko, Elena
Bioprospecting of Sea Anemones (Cnidaria, Anthozoa, Actiniaria) for β-Defensin-like α-Amylase Inhibitors
title Bioprospecting of Sea Anemones (Cnidaria, Anthozoa, Actiniaria) for β-Defensin-like α-Amylase Inhibitors
title_full Bioprospecting of Sea Anemones (Cnidaria, Anthozoa, Actiniaria) for β-Defensin-like α-Amylase Inhibitors
title_fullStr Bioprospecting of Sea Anemones (Cnidaria, Anthozoa, Actiniaria) for β-Defensin-like α-Amylase Inhibitors
title_full_unstemmed Bioprospecting of Sea Anemones (Cnidaria, Anthozoa, Actiniaria) for β-Defensin-like α-Amylase Inhibitors
title_short Bioprospecting of Sea Anemones (Cnidaria, Anthozoa, Actiniaria) for β-Defensin-like α-Amylase Inhibitors
title_sort bioprospecting of sea anemones (cnidaria, anthozoa, actiniaria) for β-defensin-like α-amylase inhibitors
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10604346/
https://www.ncbi.nlm.nih.gov/pubmed/37893056
http://dx.doi.org/10.3390/biomedicines11102682
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