A novel antifungal analog peptide derived from protaetiamycine
| Autor: | Jin-Kyoung Kim, Juneyoung Lee, Dong Gun Lee, Yangmee Kim, Hyun Joo Hong, Jae-Sam Hwang |
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| Rok vydání: | 2009 |
| Předmět: |
Antifungal Agents
Cell Membrane Permeability Molecular Sequence Data Peptide Microbial Sensitivity Tests Flow cytometry Defensins chemistry.chemical_compound Candida albicans medicine Potency Amino Acid Sequence Fluorescein isothiocyanate Molecular Biology Peptide sequence chemistry.chemical_classification Liposome medicine.diagnostic_test Vesicle Dextrans Cell Biology General Medicine Flow Cytometry Membrane chemistry Biochemistry Insect Proteins Peptides Oligopeptides Fluorescein-5-isothiocyanate |
| Zdroj: | Molecules and Cells. 28:473-477 |
| ISSN: | 0219-1032 1016-8478 |
| DOI: | 10.1007/s10059-009-0155-3 |
| Popis: | Previously, the 9-mer analog peptides, 9Pbw2 and 9Pbw4, were designed based on a defensin-like peptide, protaetiamycine isolated from Protaetia brevitarsis. In this study, antifungal effects of the analog peptides were investigated. The antifungal susceptibility testing exhibited that 9Pbw4 contained more potent antifungal activities than 9Pbw2. A PI influx assay confirmed the effects of the analog peptides and demonstrated that the peptides exerted their activity by a membrane-active mechanism, in an energy-independent manner. As the noteworthy potency of 9Pbw4, the mechanism(s) of 9Pbw4 were further investigated. The membrane studies, using rhodamine-labeled giant unilamellar vesicle (GUV) and fluorescein isothiocyanate (FITC)-dextran loaded liposome, suggested that the membrane-active mechanism of 9Pbw4 could have originated from the poreforming action and the radii of pores was presumed to be anywhere from 1.8 nm to 3.3 nm. These results were confirmed by 3D-flow cytometric contour-plot analysis. The present study suggests a potential of 9Pbw4 as a novel antifungal peptide. |
| Databáze: | OpenAIRE |
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