Abstract
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.
Original language | English |
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Pages (from-to) | 1047-1050 |
Number of pages | 4 |
Journal | Biotechnology Letters |
Volume | 21 |
Issue number | 12 |
DOIs | |
State | Published - 1999 |
Keywords
- Antifungal mechanism
- Candida albicans
- Confocal microscopy
- Ib-AMP1