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Title 

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

Authors 

Dong Gun LeeZhe Zhu JinCheol Young MaengSong Yub ShinMoo Yeol SeoKil Lyong KimKyung Soo Hahm

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

1999

Citation 

Journal of Microbiology and Biotechnology, vol. 9, no. 2, pp. 168-172

Keywords 

Cecropin AmelittinAspergillus fumigatus

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.

ISSN 

1017-7825

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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