Antifungal mechanism of a cysteine-rich antimicrobial peptide, Ib-AMP1, from Impatiens balsamina against Candida albicans

The antifungal mechanism of a 20-mer peptide, Ib-AMP1, derived from Impatiens balsamina was investigated. The oxidized (disulfide bridged) Ib-AMP1 showed a 4-fold increase in antifungal activity against Aspergillus flavus and Candida albicans than reduced (non-disulfide bridged) Ib-AMP1. Ib-AMP1 had...

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Bibliographic Details
Published in:Biotechnology letters 1999-12, Vol.21 (12), p.1047-1050
Main Authors: DONG GUN LEE, SONG YUB SHIN, KIM, D.-H, MOO YEOL SEO, JOO HYUN KANG, LEE, Y, KIL LYONG KIM, HAHM, K.-S
Format: Article
Language:English
Subjects:
Action of physical and chemical agents
Antibiotics. Antiinfectious agents. Antiparasitic agents
Antifungal agents
Aspergillus flavus
Bacteria
Biological and medical sciences
Candida albicans
Fundamental and applied biological sciences. Psychology
Impatiens balsamina
Medical sciences
Microbiology
Mycology
peptide Ib-AMP1
Peptides
Pharmacology. Drug treatments
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Summary:The antifungal mechanism of a 20-mer peptide, Ib-AMP1, derived from Impatiens balsamina was investigated. The oxidized (disulfide bridged) Ib-AMP1 showed a 4-fold increase in antifungal activity against Aspergillus flavus and Candida albicans than reduced (non-disulfide bridged) Ib-AMP1. Ib-AMP1 had very low activity for phospholipid disruption when compared with cecropin A(1-8)-magainin 2(1-12), a α-helical amphiphatic, antimicrobial peptide. Confocal microscopy showed that Ib-AMP1 binds on cell surface or penetrates into cell membranes. These results suggested that Ib-AMP1 may manifest its antifungal activity against Candida albicans by inhibiting a distinct cellular process rather than ion channel or pore formation in cell membrane.[PUBLICATION ABSTRACT]
ISSN:0141-5492
1573-6776
DOI:10.1023/A:1005636610512