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

@article{Lee2004StructureAF,
  title={Structure and fungicidal activity of a synthetic antimicrobial peptide, P18, and its truncated peptides},
  author={Dong Gun Lee and Kyung-soo Hahm and Song Yub Shin},
  journal={Biotechnology Letters},
  year={2004},
  volume={26},
  pages={337-341}
}
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… CONTINUE READING

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