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J Biol Chem, Vol. 273, Issue 42, 27438-27448, October 16, 1998
From the Department of Biochemistry, Hong Kong University of
Science and Technology, Clear Water Bay, Kowloon, Hong Kong
A natural antibacterial peptide, cecropin B (CB),
and designed analogs, CB-1 and CB-3, were synthesized. The three
peptides have different structural characteristics, with CB having one hydrophobic and one amphipathic
The Dependence of Membrane Permeability by the Antibacterial
Peptide Cecropin B and Its Analogs, CB-1 and CB-3, on Liposomes of
Different Composition
-helix, CB-1 having two amphipathic -helices, and CB-3 having two hydrophobic -helices. These
differences were used as the rationale for a study of their efficacy in
breaking liposomes with different combinations of phosphatidic acid and phosphatidylcholine. Biosensor binding measurements and encapsulating dye leakage studies showed that the higher binding affinity of CB and
CB-1 to the polar heads of lipids is not necessary for the peptides to
be more effective at lysing lipid bilayers, especially when liposomes
have a higher phosphatidic acid content. Kinetic studies, by intrinsic
and extrinsic fluorescence stopped-flow measurements, revealed two
transitional steps in liposome breakage by CB and CB-1, although only
one kinetic step was found for CB-3. Circular dichroism stopped-flow
measurements, monitoring the formation of secondary structure in the
peptides, found one kinetic step for the interaction of all of the
peptides with the liposomes. Also, the -helical motif of the
peptides was maintained after interacting with the liposomes. Based on
these results, the mechanisms of liposome lysis by CB, CB-1, and CB-3
are discussed.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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