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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 18, Number 1
BKCSDE 18(1)
January 20, 1997 

Conformation and Biological Activity of Mastoparan B and Its Analogs I
Nam Gyu Park, Jung-Kil Seo, Hee-Jung Ku, Sannamu Lee, Gohsuke Sugihara, Kwang-Ho Kim, Jang-Su Park, Shin-Won Kang
The mode of action of mastoparan B, an antimicrobial cationic tetradecapeptide amide isolated from the hornet Vespa basalis, toward phospholipid bilayers was studied with synthetic mastoparan B and its analogs with individual Ala instead of hydrophobic amino acids (1-Ile, 3-Leu, 6-Leu, 7-Val, 9-Trp, 13-Val, 14-Leu) in mastoparan B. Mastoparan B and its analogs were synthesized by the solid-phase method. Circular dichroism spectra showed that mastoparan B and its analogs adopted an unordered structure in buffer solution. In the presence of neutral and acidic liposomes, most of the peptides took an α-helical structure. The calcein leakage experiment indicated that mastoparan B interacted strongly with neutral and acidic lipid bilayers than its analogs. Mastoparan B also showed a more or less highly antimicrobial activity and hemolytic activity for human erythrocytes than its analogs. These results indicate that the hydrophobic face in the amphipathic α-helix of mastoparan B critically affect biological activity and helical contents.
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