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

Dong Gun Lee; Song Yub Shin; Dae Hee Kim; Moo Yeol Seo; Joo Hyun Kang; Younghoon Lee; Kil Lyong Kim; Kyung Soo Hahm

doi:10.1023/A:1005636610512

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

Dong Gun Lee
, Song Yub Shin
, Dae Hee Kim
, Moo Yeol Seo
, Joo Hyun Kang
, Younghoon Lee
, Kil Lyong Kim
, Kyung Soo Hahm

Research output: Contribution to journal › Article › peer-review

40 Scopus citations

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
Pages (from-to)	1047-1050
Number of pages	4
Journal	Biotechnology Letters
Volume	21
Issue number	12
DOIs	https://doi.org/10.1023/A:1005636610512
State	Published - 1999

Keywords

Antifungal mechanism
Candida albicans
Confocal microscopy
Ib-AMP1

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

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.",

keywords = "Antifungal mechanism, Candida albicans, Confocal microscopy, Ib-AMP1",

author = "Lee, \{Dong Gun\} and Shin, \{Song Yub\} and Kim, \{Dae Hee\} and Seo, \{Moo Yeol\} and Kang, \{Joo Hyun\} and Younghoon Lee and Kim, \{Kil Lyong\} and Hahm, \{Kyung Soo\}",

year = "1999",

doi = "10.1023/A:1005636610512",

language = "English",

volume = "21",

pages = "1047--1050",

journal = "Biotechnology Letters",

issn = "0141-5492",

publisher = "Springer Science and Business Media B.V.",

number = "12",

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TY - JOUR

T1 - Antifungal mechanism of a cysteine-rich antimicrobial peptide, Ib-AMP1, from Impatiens balsamina against Candida albicans

AU - Lee, Dong Gun

AU - Shin, Song Yub

AU - Kim, Dae Hee

AU - Seo, Moo Yeol

AU - Kang, Joo Hyun

AU - Lee, Younghoon

AU - Kim, Kil Lyong

AU - Hahm, Kyung Soo

PY - 1999

Y1 - 1999

N2 - 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.

AB - 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.

KW - Antifungal mechanism

KW - Candida albicans

KW - Confocal microscopy

KW - Ib-AMP1

UR - https://www.scopus.com/pages/publications/0033383178

U2 - 10.1023/A:1005636610512

DO - 10.1023/A:1005636610512

M3 - Article

AN - SCOPUS:0033383178

SN - 0141-5492

VL - 21

SP - 1047

EP - 1050

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 12

ER -

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

Abstract

Keywords

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