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pubmed-article:11401498pubmed:abstractTextThe antifungal activity and mechanism of a 23-mer peptide, PMAP-23, derived from pig myeloid was investigated. PMAP-23 displayed strong antifungal activity against yeast and mold. To investigate the antifungal mechanism of PMAP-23, fluorescence activated flow cytometry and confocal laser scanning microscopy were performed. Candida albicans treated with PMAP-23 showed higher fluorescence intensity by propidium iodide(PI) staining, which was similar to that of Melittin than untreated cells. Confocal microscopy showed that the peptide was located in the plasma membrane. The action of peptides against fungal cell membranes was examined by treating prepared protoplasts of C. albicans with the peptide and lipid vesicle titration test. The result showed that the peptide prevented the regeneration of fungal cell walls and induced release of the fluorescent dye trapped in the artificial membrane vesicles, indicating that the peptide exerts its antifungal activity by acting on the plasma lipid membrane.lld:pubmed
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pubmed-article:11401498pubmed:authorpubmed-author:KimH KHKlld:pubmed
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pubmed-article:11401498pubmed:copyrightInfoCopyright 2001 Academic Press.lld:pubmed
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pubmed-article:11401498pubmed:pagination570-4lld:pubmed
pubmed-article:11401498pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:11401498pubmed:articleTitleFungicidal effect of antimicrobial peptide, PMAP-23, isolated from porcine myeloid against Candida albicans.lld:pubmed
pubmed-article:11401498pubmed:affiliationResearch Center for Proteineous Materials, Department of Pharmacology, School of Medicine, Chosun University, 375 Seosuk-Dong, Kwangju, Dong-Ku, 501-759, Korealld:pubmed
pubmed-article:11401498pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11401498pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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