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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 17, Number 3
BKCSDE 17(3)
March 20, 1996 

The Interaction of Mastoparan B from Venom of a Hornet Vespa Basalis with Phospholipid Matrices
Nam Gyu Park, Yuhji Yamato*, Sannamu Lee*, Gohsuke Sugihara*, Jang-Su Park, Shin-Won Kang
Mastoparan B (MP-B) that is a novel MP isolated from the hornet Vespa basalis, was studied as compared with MP, in terms of interaction with phospholipid bilayer and antimicrobial activity. MP-B has more hydrophilic amino acid residues in hydrophilic face of amphiphilic α-helical structure than MP. The both peptides exhibited considerably different effect on interaction with lipid bilayers, e.g. their conformation in the presence of acidic and neutral liposomes, dye-release ability from encapsulated liposomes, but on the whole the interaction mode was similar. On antimicrobial activity, MP had a strong activity against Gram-positive bacteria but no against Gram negative ones. Contrary to this, MP-B had a strong activity against Gram-positive and potent against Gram-negative ones. Since both peptides have almost same residues on the hydrophobic side, such more hydrophilic surface on the molecule seems to lead to the subtle change in its interaction with membranes, resulting in the alternation in its biological activity.
239 - 244
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