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Article: Cordymin, an antifungal peptide from the medicinal fungus Cordyceps militaris
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TitleCordymin, an antifungal peptide from the medicinal fungus Cordyceps militaris
 
AuthorsWong, JH3
Ng, TB3
Wang, H4
Sze, SCW1
Zhang, KY1
Li, Q2
Lu, X3
 
KeywordsAntifungal
Cordyceps
Isolation
 
Issue Date2011
 
PublisherUrban und Fischer Verlag. The Journal's web site is located at http://www.elsevier.com/locate/phytomed
 
CitationPhytomedicine, 2011, v. 18 n. 5, p. 387-392 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.phymed.2010.07.010
 
AbstractCordymin, an antifungal peptide with a molecular mass of 10,906 Da and an N-terminal amino acid sequence distinct from those of previously reported proteins, was purified from the medicinal mushroom Cordyceps militaris. The isolation protocol comprised ion exchange chromatography of the aqueous extract on SP-Sepharose and Mono S and gel filtration on Superdex 75 by a fast protein liquid chromatography system. Cordymin was adsorbed on both cation exchangers. The peptide inhibited mycelial growth in Bipolaris maydis, Mycosphaerella arachidicola, Rhizoctonia solani and Candida albicans with an IC 50 of 50 μM, 10 μM, 80 μM, and 0.75 mM, respectively. However, there was no effect on Aspergillus fumigatus, Fusarium oxysporum and Valsa mali when tested up to 2 mM. The antifungal activity of the peptide was stable up to 100 °C and in the pH range 6-13, and unaffected by 10 mM Zn 2+ and 10 mM Mg 2+. Cordymin inhibited HIV-1 reverse transcriptase with an IC 50 of 55 μM. Cordymin displayed antiproliferative activity toward breast cancer cells (MCF-7) but there was no effect on colon cancer cells (HT-29). There was no mitogenic activity toward mouse spleen cells and no nitric oxide inducing activity toward mouse macrophages when tested up to 1 mM. © 2010 Elsevier GmbH.
 
ISSN0944-7113
2012 Impact Factor: 2.972
2012 SCImago Journal Rankings: 0.952
 
DOIhttp://dx.doi.org/10.1016/j.phymed.2010.07.010
 
ISI Accession Number IDWOS:000290073100010
Funding AgencyGrant Number
Medicine Panel, CUHK Research Committee
Funding Information:

The award of a direct grant from the Medicine Panel, CUHK Research Committee is gratefully acknowledged.

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorWong, JH
 
dc.contributor.authorNg, TB
 
dc.contributor.authorWang, H
 
dc.contributor.authorSze, SCW
 
dc.contributor.authorZhang, KY
 
dc.contributor.authorLi, Q
 
dc.contributor.authorLu, X
 
dc.date.accessioned2011-07-27T01:35:06Z
 
dc.date.available2011-07-27T01:35:06Z
 
dc.date.issued2011
 
dc.description.abstractCordymin, an antifungal peptide with a molecular mass of 10,906 Da and an N-terminal amino acid sequence distinct from those of previously reported proteins, was purified from the medicinal mushroom Cordyceps militaris. The isolation protocol comprised ion exchange chromatography of the aqueous extract on SP-Sepharose and Mono S and gel filtration on Superdex 75 by a fast protein liquid chromatography system. Cordymin was adsorbed on both cation exchangers. The peptide inhibited mycelial growth in Bipolaris maydis, Mycosphaerella arachidicola, Rhizoctonia solani and Candida albicans with an IC 50 of 50 μM, 10 μM, 80 μM, and 0.75 mM, respectively. However, there was no effect on Aspergillus fumigatus, Fusarium oxysporum and Valsa mali when tested up to 2 mM. The antifungal activity of the peptide was stable up to 100 °C and in the pH range 6-13, and unaffected by 10 mM Zn 2+ and 10 mM Mg 2+. Cordymin inhibited HIV-1 reverse transcriptase with an IC 50 of 55 μM. Cordymin displayed antiproliferative activity toward breast cancer cells (MCF-7) but there was no effect on colon cancer cells (HT-29). There was no mitogenic activity toward mouse spleen cells and no nitric oxide inducing activity toward mouse macrophages when tested up to 1 mM. © 2010 Elsevier GmbH.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationPhytomedicine, 2011, v. 18 n. 5, p. 387-392 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.phymed.2010.07.010
 
dc.identifier.doihttp://dx.doi.org/10.1016/j.phymed.2010.07.010
 
dc.identifier.epage392
 
dc.identifier.hkuros188258
 
dc.identifier.isiWOS:000290073100010
Funding AgencyGrant Number
Medicine Panel, CUHK Research Committee
Funding Information:

The award of a direct grant from the Medicine Panel, CUHK Research Committee is gratefully acknowledged.

 
dc.identifier.issn0944-7113
2012 Impact Factor: 2.972
2012 SCImago Journal Rankings: 0.952
 
dc.identifier.issue5
 
dc.identifier.openurl
 
dc.identifier.pmid20739167
 
dc.identifier.scopuseid_2-s2.0-79952737572
 
dc.identifier.spage387
 
dc.identifier.urihttp://hdl.handle.net/10722/135436
 
dc.identifier.volume18
 
dc.languageeng
 
dc.publisherUrban und Fischer Verlag. The Journal's web site is located at http://www.elsevier.com/locate/phytomed
 
dc.publisher.placeGermany
 
dc.relation.ispartofPhytomedicine
 
dc.relation.referencesReferences in Scopus
 
dc.subjectAntifungal
 
dc.subjectCordyceps
 
dc.subjectIsolation
 
dc.titleCordymin, an antifungal peptide from the medicinal fungus Cordyceps militaris
 
dc.typeArticle
 
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<contributor.author>Sze, SCW</contributor.author>
<contributor.author>Zhang, KY</contributor.author>
<contributor.author>Li, Q</contributor.author>
<contributor.author>Lu, X</contributor.author>
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Author Affiliations
  1. The University of Hong Kong Li Ka Shing Faculty of Medicine
  2. The University of Hong Kong
  3. Chinese University of Hong Kong
  4. China Agricultural University