Publisher : The Korean Environmental Sciences Society
DOI : 10.5322/JES.2003.12.1.077
Title & Authors
Analysis of the Interactive Characteristic of Environmental Toxic Peptide and Phospholipid ;;;
The interaction of mastoparan B, a cationic tetradecapeptide amide isolated from the hornet Vespa basalis, with phospholipid bilayers was studied with synthetic mastoparan B and its analogue with Ala instead of hydrophobic 12th amino acid residue in mastoparan B. MP-B and its derivative, [12-Ala]MP-B were synthesized by the solid-phase peptide synthesis method. MP-B and its analogue, [12-Ala]MP-B adopted an unordered structure in buffer solution. In the presence of neutral and acidic liposomes, the peptides took an -helical structure. The two peptides interacted with neutral and acidic lipid bilayers. These results indicated that the hydrophobic face in the amphipathic -helix of MP-B critically affected the biological activity and helical content.
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