Bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties

Antimicrobial peptides have attracted attention as alternatives to conventional antibiotics. Previously, a novel antimicrobial peptide, melectin, consisting of 18 amino acids was isolated from the venom of a bee, Melecta albifrons. Here, we investigated the antibacterial activity of melectin against...

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Autores principales: Ko, Su Jin, Park, Eunji, Asandei, Alina, Choi, Jee-Young, Lee, Seung-Chul, Seo, Chang Ho, Luchian, Tudor, Park, Yoonkyung
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7311438/
https://www.ncbi.nlm.nih.gov/pubmed/32576874
http://dx.doi.org/10.1038/s41598-020-66995-7
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author Ko, Su Jin
Park, Eunji
Asandei, Alina
Choi, Jee-Young
Lee, Seung-Chul
Seo, Chang Ho
Luchian, Tudor
Park, Yoonkyung
author_facet Ko, Su Jin
Park, Eunji
Asandei, Alina
Choi, Jee-Young
Lee, Seung-Chul
Seo, Chang Ho
Luchian, Tudor
Park, Yoonkyung
author_sort Ko, Su Jin
collection PubMed
description Antimicrobial peptides have attracted attention as alternatives to conventional antibiotics. Previously, a novel antimicrobial peptide, melectin, consisting of 18 amino acids was isolated from the venom of a bee, Melecta albifrons. Here, we investigated the antibacterial activity of melectin against drug-resistant bacteria. Melectin showed broad-spectrum antimicrobial activity but low cytotoxicity and no hemolytic activity. Melectin maintained its antimicrobial activity at physiological salt concentrations. Melectin is an α-helical structure that binds to the bacterial membrane via electrostatic interactions and kills bacteria in a short time by bacterial membrane targeting. Collectively, our results suggest that melectin has antibacterial activity and anti-inflammatory activity.
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spelling pubmed-73114382020-06-25 Bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties Ko, Su Jin Park, Eunji Asandei, Alina Choi, Jee-Young Lee, Seung-Chul Seo, Chang Ho Luchian, Tudor Park, Yoonkyung Sci Rep Article Antimicrobial peptides have attracted attention as alternatives to conventional antibiotics. Previously, a novel antimicrobial peptide, melectin, consisting of 18 amino acids was isolated from the venom of a bee, Melecta albifrons. Here, we investigated the antibacterial activity of melectin against drug-resistant bacteria. Melectin showed broad-spectrum antimicrobial activity but low cytotoxicity and no hemolytic activity. Melectin maintained its antimicrobial activity at physiological salt concentrations. Melectin is an α-helical structure that binds to the bacterial membrane via electrostatic interactions and kills bacteria in a short time by bacterial membrane targeting. Collectively, our results suggest that melectin has antibacterial activity and anti-inflammatory activity. Nature Publishing Group UK 2020-06-23 /pmc/articles/PMC7311438/ /pubmed/32576874 http://dx.doi.org/10.1038/s41598-020-66995-7 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Ko, Su Jin
Park, Eunji
Asandei, Alina
Choi, Jee-Young
Lee, Seung-Chul
Seo, Chang Ho
Luchian, Tudor
Park, Yoonkyung
Bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties
title Bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties
title_full Bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties
title_fullStr Bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties
title_full_unstemmed Bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties
title_short Bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties
title_sort bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7311438/
https://www.ncbi.nlm.nih.gov/pubmed/32576874
http://dx.doi.org/10.1038/s41598-020-66995-7
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