Antifungal activities of peptides with the sequence 10-17 of magainin 2 at the N-termini against Aspergillus fumigatus

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dc.contributor.authorMyung Kyu Lee-
dc.contributor.authorDong Gun Lee-
dc.contributor.authorSong Yub Shin-
dc.contributor.authorSung Gu Lee-
dc.contributor.authorJoo Hyun Kang-
dc.contributor.authorKyung Soo Hahm-
dc.date.accessioned2017-04-19T08:45:40Z-
dc.date.available2017-04-19T08:45:40Z-
dc.date.issued1996-
dc.identifier.issn1225-8873-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/3847-
dc.description.abstractTwo peptides, MA-inv and MA-ME, with the sequence 10-17 of magainin 2 at their N-termini were designed and synthesized. The peptides had higher antifungal activities against Aspergillus fumigatus without hemolytic activities. The minimal inhibition concentratory (MIC) values of both peptides against A. fumigatus were 5 μg/ml, whereas those of the native peptides, magainin 2 and melittin, were 10 μg/ml. At 3 μg/ml, MA-inv and MA-ME inhibited the mycelium growth of A. fumigatus by 94.6% and 97.3%, respectively, whereas magainin 2 and melittin inhibited by 62.2% and 32.4%, respectively. MA-inv showed up to 80% inhibition of (1,3)-β-D-glucan synthase activity of A. fumigatus. The peptides also showed antifungal activities for other fungi of Aspergillus sp. However, the antibiotic activities of MA-ME against Escherichia coli, Bacillus subtilis and Fusarium oxysporum were more effective than those of MA-inv, suggesting that the C-terminal sequences of MA-inv and MA-ME may also influence their antibiotic activities. These results suggest that the N-terminal sequence of the designed peptides, KKFGKAFV, is important for their antifungal activities against A. fumigatus and their C-terminal sequences are related to the organism selectivity.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleAntifungal activities of peptides with the sequence 10-17 of magainin 2 at the N-termini against Aspergillus fumigatus-
dc.title.alternativeAntifungal activities of peptides with the sequence 10-17 of magainin 2 at the N-termini against Aspergillus fumigatus-
dc.typeArticle-
dc.citation.titleJournal of Microbiology-
dc.citation.number3-
dc.citation.endPage278-
dc.citation.startPage274-
dc.citation.volume34-
dc.contributor.affiliatedAuthorMyung Kyu Lee-
dc.contributor.affiliatedAuthorDong Gun Lee-
dc.contributor.affiliatedAuthorSong Yub Shin-
dc.contributor.affiliatedAuthorSung Gu Lee-
dc.contributor.affiliatedAuthorJoo Hyun Kang-
dc.contributor.affiliatedAuthorKyung Soo Hahm-
dc.contributor.alternativeName이명규-
dc.contributor.alternativeName이동건-
dc.contributor.alternativeName신송엽-
dc.contributor.alternativeName이성구-
dc.contributor.alternativeName강주현-
dc.contributor.alternativeName함경수-
dc.identifier.bibliographicCitationJournal of Microbiology, vol. 34, no. 3, pp. 274-278-
dc.subject.keywordAntifungal activity-
dc.subject.keywordAspergillus fumigatus-
dc.subject.keywordGlucan synthase-
dc.subject.keywordMagainin 2 derived peptide-
dc.subject.keywordSynthetic peptide-
dc.subject.localAnti-fungal activity-
dc.subject.localAntifungal activity-
dc.subject.localantifungal activity-
dc.subject.localAspergillus fumigatus-
dc.subject.localGlucan synthase-
dc.subject.localMagainin 2 derived peptide-
dc.subject.localSynthetic peptide-
dc.subject.localSynthetic peptides-
dc.subject.localsynthetic peptide-
dc.description.journalClassY-
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