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Biophysical Journal 45: 1079-1083 (1984)
© 1984 the Biophysical Society

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Melittin and the 8-26 fragment. Differences in ionophoric properties as measured by monolayer method.

V S Gevod and K S Birdi

ABSTRACT

Melittin is a major (approximately 50%) protein component of bee venom. This peptide is an amphiphilic protein, because, while the amino acid residues 1-20 are predominantly hydrophobic (with the exception of Lys-7), residues 21-26 are hydrophilic. The binding properties to vesicles and lipid bilayers of melittin have provided much useful information regarding biological (hemolytic) activity (Habermann, E., 1972, Science [Wash. DC], 177:314-322). Recent studies have convincingly established that the melittin monolayer (at air-water interface) model membrane system allows one to analyze the various forces present in such structures. We present comparative monolayer studies of melittin and the peptide fragment 8-26 regarding the channel formation for the selective anion (Cl-) penetration in monolayers, analogous to melittin (tetramer) channel function in lipid bilayer. The differences in surface pressure and surface potential of monolayers between native melittin and the 8-26 fragment suggest that these may be ascribed to Lys-7.




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N. Asthana, S. P. Yadav, and J. K. Ghosh
Dissection of Antibacterial and Toxic Activity of Melittin: A LEUCINE ZIPPER MOTIF PLAYS A CRUCIAL ROLE IN DETERMINING ITS HEMOLYTIC ACTIVITY BUT NOT ANTIBACTERIAL ACTIVITY
J. Biol. Chem., December 31, 2004; 279(53): 55042 - 55050.
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Copyright © 1984 by the Biophysical Society.