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Campesin, a thermostable antifungal peptide with highly potent antipathogenic activities
An 9.4-kDa antifungal peptide designated as campesin was isolated from seeds of the cabbage Brassica campestris. The isolation procedure involved affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Q-Sepharose and Mono S, and gel filtration on Superdex 75 and Superdex Peptid...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Society for Biotechnology, Japan. Published by Elsevier B.V.
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7106469/ https://www.ncbi.nlm.nih.gov/pubmed/19664563 http://dx.doi.org/10.1016/j.jbiosc.2009.03.013 |
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author | Lin, Peng Wong, Jack Ho Xia, Lixin Ng, Tzi Bun |
author_facet | Lin, Peng Wong, Jack Ho Xia, Lixin Ng, Tzi Bun |
author_sort | Lin, Peng |
collection | PubMed |
description | An 9.4-kDa antifungal peptide designated as campesin was isolated from seeds of the cabbage Brassica campestris. The isolation procedure involved affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Q-Sepharose and Mono S, and gel filtration on Superdex 75 and Superdex Peptide. The peptide was adsorbed on the first three chromatographic media. It exerted an inhibitory action on mycelial growth including Fusarium oxysporum and Mycosphaerella arachidicola, with an IC(50) of 5.1 μM and 4.4 μM, respectively. The peptide was characterized by remarkable thermostability and pH stability. It inhibited proliferation of HepG2 and MCF cancer cells with an IC(50) of 6.4 μM and 1.8 μM, and the activity of HIV-1 reverse transcriptase with an IC(50) of 3.2 μM. It demonstrated lysolecithin binding activity. |
format | Online Article Text |
id | pubmed-7106469 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | The Society for Biotechnology, Japan. Published by Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71064692020-03-31 Campesin, a thermostable antifungal peptide with highly potent antipathogenic activities Lin, Peng Wong, Jack Ho Xia, Lixin Ng, Tzi Bun J Biosci Bioeng Article An 9.4-kDa antifungal peptide designated as campesin was isolated from seeds of the cabbage Brassica campestris. The isolation procedure involved affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Q-Sepharose and Mono S, and gel filtration on Superdex 75 and Superdex Peptide. The peptide was adsorbed on the first three chromatographic media. It exerted an inhibitory action on mycelial growth including Fusarium oxysporum and Mycosphaerella arachidicola, with an IC(50) of 5.1 μM and 4.4 μM, respectively. The peptide was characterized by remarkable thermostability and pH stability. It inhibited proliferation of HepG2 and MCF cancer cells with an IC(50) of 6.4 μM and 1.8 μM, and the activity of HIV-1 reverse transcriptase with an IC(50) of 3.2 μM. It demonstrated lysolecithin binding activity. The Society for Biotechnology, Japan. Published by Elsevier B.V. 2009-09 2009-08-05 /pmc/articles/PMC7106469/ /pubmed/19664563 http://dx.doi.org/10.1016/j.jbiosc.2009.03.013 Text en Copyright © 2009 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Lin, Peng Wong, Jack Ho Xia, Lixin Ng, Tzi Bun Campesin, a thermostable antifungal peptide with highly potent antipathogenic activities |
title | Campesin, a thermostable antifungal peptide with highly potent antipathogenic activities |
title_full | Campesin, a thermostable antifungal peptide with highly potent antipathogenic activities |
title_fullStr | Campesin, a thermostable antifungal peptide with highly potent antipathogenic activities |
title_full_unstemmed | Campesin, a thermostable antifungal peptide with highly potent antipathogenic activities |
title_short | Campesin, a thermostable antifungal peptide with highly potent antipathogenic activities |
title_sort | campesin, a thermostable antifungal peptide with highly potent antipathogenic activities |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7106469/ https://www.ncbi.nlm.nih.gov/pubmed/19664563 http://dx.doi.org/10.1016/j.jbiosc.2009.03.013 |
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