Antifungal mechanism of antifungal peptide derived from cecropin A(1- 8)-melittin(1-12) hybrid against Aspergillus fumigatus

Dong Gun Lee, Zhe Zhu Jin, Cheol Young Maeng, Song Yub Shin, Moo Yeol Seo, Kil Lyong Kim, Kyung Soo Hahm

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The antifungal mechanism of the antifungal peptide against Aspergillus fumigatus, K18, 19CA-(1-8)-ME(1-12), derived from cecropin A(1-8)- melittin(1-12) was investigated by confocal laser scanning microscopy, cell wall regeneration, ATPase activity inhibition, and released potassium ion. By confocal laser scanning microscopy, K18, 19-CA(1-8)-ME(1-12) was detected on the surface of A. fumigatus, while cecropin A used as a negative control peptide was not detected. The protoplast of A. fumigatus treated with K18, 19-CA(1-8)-ME(1-12) failed to regenerate the fungal cell walls. Compared with cecropin A, the amount of potassium ion released by K18, 19-CA(1-8)-ME(1-12) was increased. Furthermore, K18, 19-CA(1-8)-ME(1- 12) inhibited the ATPase activity on the plasma membrane. These results suggested that K18, 19-CA(1-8)-ME (1-12) acts on the plasma membrane of A. fumigatus and its antifungal action is due to the ion channel or pore formation on the plasma membrane.

Original languageEnglish
Pages (from-to)168-172
Number of pages5
JournalJournal of Microbiology and Biotechnology
Volume9
Issue number2
StatePublished - Apr 1999

Keywords

  • Aspergillus fumigatus
  • Cecropin A
  • Melittin

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