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

Cited 0 time in scopus
Metadata Downloads
Title
Antifungal mechanism of antifungal peptide derived from cecropin A(1-8)-melittin(1-12) hybrid against Aspergillus fumigatus
Author(s)
Dong Gun Lee; Zhe Zhu Jin; Cheol Young Maeng; Song Yub Shin; Moo Yeol Seo; Kil Lyong Kim; Kyung Soo Hahm
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 9, no. 2, pp. 168-172
Publication Year
1999
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.
Keyword
Cecropin AmelittinAspergillus fumigatus
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.