Structure and fungicidal activity of a synthetic antimicrobial peptide, P18, and its truncated peptides

Dong Gun Lee; Kyung Soo Hahm; Song Yub Shin

doi:10.1023/B:BILE.0000015472.09542.6d

Structure and fungicidal activity of a synthetic antimicrobial peptide, P18, and its truncated peptides

Dong Gun Lee, Kyung Soo Hahm, Song Yub Shin

Chosun University

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

34 Scopus citations

Abstract

P18 (KWKLFKKIPKFLHLAKKF-NH₂) is an antimicrobial peptide designed from a cecropin A-magainin 2 hybrid that has potent antibacterial activity without hemolytic activity against human erythrocytes. In this study, P18 displayed potent fungicidal activity (MIC: 12.5-25 μM) against pathogenic fungi, Candida albicans, Trichosporon beigelii, Aspergillus flavus and Fusarium oxysporum. The central Pro⁹ residue and the entire sequence of P18 are essential for its full fungicidal activity. Circular dichroism analysis suggested that the higher α-helical content of the peptides did not correlate with the stronger fungicidal activity.

Original language	English
Pages (from-to)	337-341
Number of pages	5
Journal	Biotechnology Letters
Volume	26
Issue number	4
DOIs	https://doi.org/10.1023/B:BILE.0000015472.09542.6d
State	Published - Feb 2004

Keywords

α-helicity
Fungicidal activity
P18
Truncated peptide

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10.1023/B:BILE.0000015472.09542.6d

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abstract = "P18 (KWKLFKKIPKFLHLAKKF-NH2) is an antimicrobial peptide designed from a cecropin A-magainin 2 hybrid that has potent antibacterial activity without hemolytic activity against human erythrocytes. In this study, P18 displayed potent fungicidal activity (MIC: 12.5-25 μM) against pathogenic fungi, Candida albicans, Trichosporon beigelii, Aspergillus flavus and Fusarium oxysporum. The central Pro9 residue and the entire sequence of P18 are essential for its full fungicidal activity. Circular dichroism analysis suggested that the higher α-helical content of the peptides did not correlate with the stronger fungicidal activity.",

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AU - Lee, Dong Gun

AU - Hahm, Kyung Soo

AU - Shin, Song Yub

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N2 - P18 (KWKLFKKIPKFLHLAKKF-NH2) is an antimicrobial peptide designed from a cecropin A-magainin 2 hybrid that has potent antibacterial activity without hemolytic activity against human erythrocytes. In this study, P18 displayed potent fungicidal activity (MIC: 12.5-25 μM) against pathogenic fungi, Candida albicans, Trichosporon beigelii, Aspergillus flavus and Fusarium oxysporum. The central Pro9 residue and the entire sequence of P18 are essential for its full fungicidal activity. Circular dichroism analysis suggested that the higher α-helical content of the peptides did not correlate with the stronger fungicidal activity.

AB - P18 (KWKLFKKIPKFLHLAKKF-NH2) is an antimicrobial peptide designed from a cecropin A-magainin 2 hybrid that has potent antibacterial activity without hemolytic activity against human erythrocytes. In this study, P18 displayed potent fungicidal activity (MIC: 12.5-25 μM) against pathogenic fungi, Candida albicans, Trichosporon beigelii, Aspergillus flavus and Fusarium oxysporum. The central Pro9 residue and the entire sequence of P18 are essential for its full fungicidal activity. Circular dichroism analysis suggested that the higher α-helical content of the peptides did not correlate with the stronger fungicidal activity.

KW - α-helicity

KW - Fungicidal activity

KW - P18

KW - Truncated peptide

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AN - SCOPUS:1442338547

SN - 0141-5492

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SP - 337

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JO - Biotechnology Letters

JF - Biotechnology Letters

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ER -

Structure and fungicidal activity of a synthetic antimicrobial peptide, P18, and its truncated peptides

Abstract

Keywords

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