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

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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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References

  • Boman HG, Hultmark D (1987) Cell-free immunity in insects. Annu. Rev. Microbiol. 41: 103–126.

    Google Scholar 

  • Chen YH, Yang JT, Chau KH (1974) Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry 13: 3350–3359.

    Google Scholar 

  • Dathe M, Wieprecht T, Nikolenko H, Handel L, Maloy WL, Mac-Donald DL, Beyermann M, Bienert M (1997) Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Lett. 403: 208–212.

    Google Scholar 

  • Gesell J, Zasloff M, Opella SJ (1997) Two-dimensional 1 H NMR experiments show that the 23-residue magainin antibiotic peptide is an ?-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. J. Biomol. NMR 9: 127–135.

    Google Scholar 

  • Holak TA, Engstrom A, Kraulis PJ, Lindeberg G, Bennich H, Jones TA, Gronenborn AM, Clore GM (1988) The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry 27: 7620–7629.

    Google Scholar 

  • Mosmann T (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Meth. 80: 14–20.

    Google Scholar 

  • Oh D, Shin SY, Lee S, Kang JH, Kim SD, Ryu PD, Hahm KS, Kim Y (2000) Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures. Biochemistry 39: 11855–11864.

    Google Scholar 

  • Sheppard RC (1980) New solid-phase methods in the synthesis of natural peptides. Biochem. Soc. Trans. 8: 744–747.

    Google Scholar 

  • Shin SY, Kang JH, Hahm K-S (1999) Structure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melittin hybrid peptides J. Pept. Res. 53: 82–90.

    Google Scholar 

  • Shin SY, Lee SH, Yang S-T, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm K-S, Kim JI (2001) Antibacterial, antitumor and hemolytic activities of ?-helical antibiotic peptide, P18 and its analogs. J. Pept. Res. 58: 504–514.

    Google Scholar 

  • Soravia E, Martini G, Zasloff M (1988) Antimicrobial properties of peptides from Xenopus granular gland secretions. FEBS Lett. 228: 337–340.

    Google Scholar 

  • Steiner H, Andreu D, Merrifield RB (1988) Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects. Biochim. Biophys. Acta 939: 260–266.

    Google Scholar 

  • Zasloff M (1987) Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 84: 5449–5453.

    Google Scholar 

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Lee, D.G., Hahm, KS. & Shin, S.Y. Structure and fungicidal activity of a synthetic antimicrobial peptide, P18, and its truncated peptides. Biotechnology Letters 26, 337–341 (2004). https://doi.org/10.1023/B:BILE.0000015472.09542.6d

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  • DOI: https://doi.org/10.1023/B:BILE.0000015472.09542.6d

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