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Magnificamide, a β-Defensin-Like Peptide from the Mucus of the Sea Anemone Heteractis magnifica, Is a Strong Inhibitor of Mammalian α-Amylases
Sea anemones’ venom is rich in peptides acting on different biological targets, mainly on cytoplasmic membranes and ion channels. These animals are also a source of pancreatic α-amylase inhibitors, which have the ability to control the glucose level in the blood and can be used for the treatment of...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6835510/ https://www.ncbi.nlm.nih.gov/pubmed/31546678 http://dx.doi.org/10.3390/md17100542 |
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author | Sintsova, Oksana Gladkikh, Irina Kalinovskii, Aleksandr Zelepuga, Elena Monastyrnaya, Margarita Kim, Natalia Shevchenko, Lyudmila Peigneur, Steve Tytgat, Jan Kozlovskaya, Emma Leychenko, Elena |
author_facet | Sintsova, Oksana Gladkikh, Irina Kalinovskii, Aleksandr Zelepuga, Elena Monastyrnaya, Margarita Kim, Natalia Shevchenko, Lyudmila Peigneur, Steve Tytgat, Jan Kozlovskaya, Emma Leychenko, Elena |
author_sort | Sintsova, Oksana |
collection | PubMed |
description | Sea anemones’ venom is rich in peptides acting on different biological targets, mainly on cytoplasmic membranes and ion channels. These animals are also a source of pancreatic α-amylase inhibitors, which have the ability to control the glucose level in the blood and can be used for the treatment of prediabetes and type 2 diabetes mellitus. Recently we have isolated and characterized magnificamide (44 aa, 4770 Da), the major α-amylase inhibitor of the sea anemone Heteractis magnifica mucus, which shares 84% sequence identity with helianthamide from Stichodactyla helianthus. Herein, we report some features in the action of a recombinant analog of magnificamide. The recombinant peptide inhibits porcine pancreatic and human saliva α-amylases with Ki’s equal to 0.17 ± 0.06 nM and 7.7 ± 1.5 nM, respectively, and does not show antimicrobial or channel modulating activities. We have concluded that the main function of magnificamide is the inhibition of α-amylases; therefore, its functionally active recombinant analog is a promising agent for further studies as a potential drug candidate for the treatment of the type 2 diabetes mellitus. |
format | Online Article Text |
id | pubmed-6835510 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-68355102019-11-25 Magnificamide, a β-Defensin-Like Peptide from the Mucus of the Sea Anemone Heteractis magnifica, Is a Strong Inhibitor of Mammalian α-Amylases Sintsova, Oksana Gladkikh, Irina Kalinovskii, Aleksandr Zelepuga, Elena Monastyrnaya, Margarita Kim, Natalia Shevchenko, Lyudmila Peigneur, Steve Tytgat, Jan Kozlovskaya, Emma Leychenko, Elena Mar Drugs Article Sea anemones’ venom is rich in peptides acting on different biological targets, mainly on cytoplasmic membranes and ion channels. These animals are also a source of pancreatic α-amylase inhibitors, which have the ability to control the glucose level in the blood and can be used for the treatment of prediabetes and type 2 diabetes mellitus. Recently we have isolated and characterized magnificamide (44 aa, 4770 Da), the major α-amylase inhibitor of the sea anemone Heteractis magnifica mucus, which shares 84% sequence identity with helianthamide from Stichodactyla helianthus. Herein, we report some features in the action of a recombinant analog of magnificamide. The recombinant peptide inhibits porcine pancreatic and human saliva α-amylases with Ki’s equal to 0.17 ± 0.06 nM and 7.7 ± 1.5 nM, respectively, and does not show antimicrobial or channel modulating activities. We have concluded that the main function of magnificamide is the inhibition of α-amylases; therefore, its functionally active recombinant analog is a promising agent for further studies as a potential drug candidate for the treatment of the type 2 diabetes mellitus. MDPI 2019-09-21 /pmc/articles/PMC6835510/ /pubmed/31546678 http://dx.doi.org/10.3390/md17100542 Text en © 2019 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Sintsova, Oksana Gladkikh, Irina Kalinovskii, Aleksandr Zelepuga, Elena Monastyrnaya, Margarita Kim, Natalia Shevchenko, Lyudmila Peigneur, Steve Tytgat, Jan Kozlovskaya, Emma Leychenko, Elena Magnificamide, a β-Defensin-Like Peptide from the Mucus of the Sea Anemone Heteractis magnifica, Is a Strong Inhibitor of Mammalian α-Amylases |
title | Magnificamide, a β-Defensin-Like Peptide from the Mucus of the Sea Anemone Heteractis magnifica, Is a Strong Inhibitor of Mammalian α-Amylases |
title_full | Magnificamide, a β-Defensin-Like Peptide from the Mucus of the Sea Anemone Heteractis magnifica, Is a Strong Inhibitor of Mammalian α-Amylases |
title_fullStr | Magnificamide, a β-Defensin-Like Peptide from the Mucus of the Sea Anemone Heteractis magnifica, Is a Strong Inhibitor of Mammalian α-Amylases |
title_full_unstemmed | Magnificamide, a β-Defensin-Like Peptide from the Mucus of the Sea Anemone Heteractis magnifica, Is a Strong Inhibitor of Mammalian α-Amylases |
title_short | Magnificamide, a β-Defensin-Like Peptide from the Mucus of the Sea Anemone Heteractis magnifica, Is a Strong Inhibitor of Mammalian α-Amylases |
title_sort | magnificamide, a β-defensin-like peptide from the mucus of the sea anemone heteractis magnifica, is a strong inhibitor of mammalian α-amylases |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6835510/ https://www.ncbi.nlm.nih.gov/pubmed/31546678 http://dx.doi.org/10.3390/md17100542 |
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