File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Cordymin, an antifungal peptide from the medicinal fungus Cordyceps militaris

TitleCordymin, an antifungal peptide from the medicinal fungus Cordyceps militaris
Authors
KeywordsAntifungal
Cordyceps
Isolation
Issue Date2011
PublisherUrban und Fischer Verlag. The Journal's web site is located at http://www.elsevier.com/locate/phytomed
Citation
Phytomedicine, 2011, v. 18 n. 5, p. 387-392 How to Cite?
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.
Persistent Identifierhttp://hdl.handle.net/10722/135436
ISSN
2014 Impact Factor: 3.126
2014 SCImago Journal Rankings: 0.930
ISI Accession Number ID
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.

References

 

DC FieldValueLanguage
dc.contributor.authorWong, JHen_HK
dc.contributor.authorNg, TBen_HK
dc.contributor.authorWang, Hen_HK
dc.contributor.authorSze, SCWen_HK
dc.contributor.authorZhang, KYen_HK
dc.contributor.authorLi, Qen_HK
dc.contributor.authorLu, Xen_HK
dc.date.accessioned2011-07-27T01:35:06Z-
dc.date.available2011-07-27T01:35:06Z-
dc.date.issued2011en_HK
dc.identifier.citationPhytomedicine, 2011, v. 18 n. 5, p. 387-392en_HK
dc.identifier.issn0944-7113en_HK
dc.identifier.urihttp://hdl.handle.net/10722/135436-
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.en_HK
dc.languageengen_US
dc.publisherUrban und Fischer Verlag. The Journal's web site is located at http://www.elsevier.com/locate/phytomeden_HK
dc.relation.ispartofPhytomedicineen_HK
dc.subjectAntifungalen_HK
dc.subjectCordycepsen_HK
dc.subjectIsolationen_HK
dc.titleCordymin, an antifungal peptide from the medicinal fungus Cordyceps militarisen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0944-7113&volume=18&issue=5&spage=387&epage=392&date=2011&atitle=Cordymin,+an+antifungal+peptide+from+the+medicinal+fungus+Cordyceps+militaris-
dc.identifier.emailSze, SCW: stephens@hku.hken_HK
dc.identifier.emailZhang, KY: ybzhang@hku.hken_HK
dc.identifier.authoritySze, SCW=rp00514en_HK
dc.identifier.authorityZhang, KY=rp01410en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.phymed.2010.07.010en_HK
dc.identifier.pmid20739167en_HK
dc.identifier.scopuseid_2-s2.0-79952737572en_HK
dc.identifier.hkuros188258en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79952737572&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume18en_HK
dc.identifier.issue5en_HK
dc.identifier.spage387en_HK
dc.identifier.epage392en_HK
dc.identifier.isiWOS:000290073100010-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridWong, JH=34874358200en_HK
dc.identifier.scopusauthoridNg, TB=35311803300en_HK
dc.identifier.scopusauthoridWang, H=7501734185en_HK
dc.identifier.scopusauthoridSze, SCW=23482617000en_HK
dc.identifier.scopusauthoridZhang, KY=23483121900en_HK
dc.identifier.scopusauthoridLi, Q=22034705700en_HK
dc.identifier.scopusauthoridLu, X=7404839049en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats