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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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2023
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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. |
format | Online Article Text |
id | pubmed-10604346 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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