Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Lin, Peng, Wong, Jack Ho, Xia, Lixin, Ng, Tzi Bun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Society for Biotechnology, Japan. Published by Elsevier B.V. 2009
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
_version_ 1783512612443521024
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
work_keys_str_mv AT linpeng campesinathermostableantifungalpeptidewithhighlypotentantipathogenicactivities
AT wongjackho campesinathermostableantifungalpeptidewithhighlypotentantipathogenicactivities
AT xialixin campesinathermostableantifungalpeptidewithhighlypotentantipathogenicactivities
AT ngtzibun campesinathermostableantifungalpeptidewithhighlypotentantipathogenicactivities