Structure-antifungal activity relationships of cecropin A hybrid peptides against Trichoderma sp.

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dc.contributor.authorSong Yub Shin-
dc.contributor.authorDong Gun Lee-
dc.contributor.authorSung Gu Lee-
dc.contributor.authorKil Lyong Kim-
dc.contributor.authorMyung Kyu Lee-
dc.contributor.authorKyung Soo Hahm-
dc.date.accessioned2017-04-19T08:54:48Z-
dc.date.available2017-04-19T08:54:48Z-
dc.date.issued1997-
dc.identifier.issn1225-8873-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4187-
dc.description.abstractThe hybrid peptides, CA-ME, CA-MA and CA-BO, with the N-terminal sequence 1-8 of cecropin A and the N-terminal sequences 1-12 of melittin, magainin 2 and bombinin, respectively, have more improved antibacterial activities. CA-MA was found to have stronger antifungal activity against Trichoderma sp than other hybrid peptides and their parental peptides. In order to elucidate the relationships between the peptide structure and antifungal activity, several analogues of CA-MA or CA-BO were also designed and synthesized by the solid phase method. Antifungal activity was measured against T. reesei and T. viride, and hemolytic activity was measured by a solution method against human red blood cells. The residue 16 of CA-MA, Ser, was found to be important for antifungal activity. When the residue was substituted with Leu, antifungal activity was dramatically decreased. CA-MA, P1, P4 and P5 designed in this study showed powerful antifungal activity against T. reesei and T. viride with low hemolytic activity against human red blood cells. These hybrid peptides will be potentially useful model to further design peptides with powerful antifungal activity for the effective therapy of fungal infection and understand the mechanisms of antifungal actions of hybrid peptides.-
dc.publisherMicrobiological Society Korea-
dc.titleStructure-antifungal activity relationships of cecropin A hybrid peptides against Trichoderma sp.-
dc.title.alternativeStructure-antifungal activity relationships of cecropin A hybrid peptides against Trichoderma sp.-
dc.typeArticle-
dc.citation.titleJournal of Microbiology-
dc.citation.number1-
dc.citation.endPage24-
dc.citation.startPage21-
dc.citation.volume35-
dc.contributor.affiliatedAuthorSong Yub Shin-
dc.contributor.affiliatedAuthorDong Gun Lee-
dc.contributor.affiliatedAuthorSung Gu Lee-
dc.contributor.affiliatedAuthorKil Lyong Kim-
dc.contributor.affiliatedAuthorMyung Kyu Lee-
dc.contributor.affiliatedAuthorKyung Soo Hahm-
dc.contributor.alternativeName신송엽-
dc.contributor.alternativeName이동건-
dc.contributor.alternativeName이성구-
dc.contributor.alternativeName김길룡-
dc.contributor.alternativeName이명규-
dc.contributor.alternativeName함경수-
dc.identifier.bibliographicCitationJournal of Microbiology, vol. 35, no. 1, pp. 21-24-
dc.subject.keywordAntifungal activity-
dc.subject.keywordCecropin A hybrid peptide-
dc.subject.keywordHemolytic activity-
dc.subject.keywordTrichoderma sp.-
dc.subject.localAntifungal activity-
dc.subject.localAnti-fungal activity-
dc.subject.localantifungal activity-
dc.subject.localCecropin A hybrid peptide-
dc.subject.localHemolytic activity-
dc.subject.localhemolytic activity-
dc.subject.localTrichoderma sp.-
dc.description.journalClassY-
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