Bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties
Abstract 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 melecti...
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2020
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oai:doaj.org-article:bcd81e0dfe3d49aa8b83f3167750b21b2021-12-02T17:45:21ZBee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties10.1038/s41598-020-66995-72045-2322https://doaj.org/article/bcd81e0dfe3d49aa8b83f3167750b21b2020-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-66995-7https://doaj.org/toc/2045-2322Abstract 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.Su Jin KoEunji ParkAlina AsandeiJee-Young ChoiSeung-Chul LeeChang Ho SeoTudor LuchianYoonkyung ParkNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-12 (2020) |
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Medicine R Science Q Su Jin Ko Eunji Park Alina Asandei Jee-Young Choi Seung-Chul Lee Chang Ho Seo Tudor Luchian Yoonkyung Park Bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties |
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Abstract 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. |
format |
article |
author |
Su Jin Ko Eunji Park Alina Asandei Jee-Young Choi Seung-Chul Lee Chang Ho Seo Tudor Luchian Yoonkyung Park |
author_facet |
Su Jin Ko Eunji Park Alina Asandei Jee-Young Choi Seung-Chul Lee Chang Ho Seo Tudor Luchian Yoonkyung Park |
author_sort |
Su Jin Ko |
title |
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_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_sort |
bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties |
publisher |
Nature Portfolio |
publishDate |
2020 |
url |
https://doaj.org/article/bcd81e0dfe3d49aa8b83f3167750b21b |
work_keys_str_mv |
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