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KMID : 0545119990090020168
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Journal of Microbiology and Biotechnology
1999 Volume.9 No. 2 p.168 ~ p.172
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Antifungal Mechanism of Antifungal Peptide Derived from Cecropin A(1-8)-Melittin(1-12)Hybrid against Aspergillus fumigatus
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Lee, Dong Gun
Jin, Zhe Zhu/Maeng, Cheol Young/Shin, Song Yub/Seo, Moo Yeol/Kim, Kil Lyong/Hahm, Kyung Soo
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Abstract
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The antifungal mechanism of the antifungal peptide against Aspetgillus fumnigatus, K^18.19-CA(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, K^18.19-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 K^18.19-CA(1-8)-ME(1-12) failed to regenerate the fungal cell walls. Compared with cecropin A, the amount of potassium ion released by K^18.19- CA(1-8)-ME(I-12) was increased. Furthennore, K^18.19-CA(1-8)-ME(1-12) inhibited the ATPase activity on the plasma membrane. These results suggested that K^18.19-CA( l-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.
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