Title Antifungal activities of peptides with the sequence 10-17 of magainin 2 at the N-termini against aspergillus fumigatus
Author Lee, Myung Kyu · Lee, Dong Gun · Shin, Song Yub · Lee, Sung Gu · Kang, Joo Hyun · Hahm, Kyung Soo *
Address Peptide Engineering Research Unit, Korea Research Institute of Bioscience and Biotechnology, KIST
Bibliography Journal of Microbiology, 34(3),274-278, 1996,
DOI
Key Words Antifungal activity, magainin 2 derived peptide, Adperfillus fumigatus, synthetic peptide, glucan synthase
Abstract Two peptides, MA-inv AND MA-ME, with the sequence 10-17 of maganin 2 at their-N-termini were designed and synthesized. The peptides had higher antifungal activities against Aspergilus fumigatus without hemolytic activities. The minimal inhibition concentratory (MIC) values of both peptides against A. fumigatus were 5 ㎍/ml, whereas those of the native peptides, magainin 2 and melittin, were 10㎍/ml. At 3 ㎍/ml, MA-inv and MA-ME inhibited the mycelium growth of A. fumigatus by 94.6% and 97.3% respectively, whereas magainin 2 and melittin inhibited by 62.2% and 32.4, respectively. MA-inv showed up to 80% inhibition of (1, 3)-β-D-glucan synthase activity of A. fumigatus. The peptides also showed up to 80% inhibition of (1, 3)-β-D glucan synthase activity of A. fumigatus. The peptides also showed antifungal activities for other fungi of Aspergillus sp. However, the antibiotic activities of MA-ME against Escherichia coli, Bacillus subtilis and Fusarium oxysporum were more effective than those of MA-inv, suggesting that the C-terminal sequences of MA-inv and MA-ME may also influence their antibiotic activities. These results suggest that the N-terminal sequence of the designed peptides, KKFGKAFV, is important for their antifungal activities against A. fumigatus and their C- terminal sequences are related to the organism selectivity.
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