The antibacterial peptide ceratotoxin A displays alamethicin-like behavior in lipid bilayers.

Abstract:

:Ceratotoxin A (CtxA), a 36-residue alpha-helical cationic peptide isolated from the medfly Ceratitis capitata, exhibits strong antibacterial activity. To determine its mode of action against bacteria, we investigated the behavior of ceratotoxin A by incorporating it into planar lipid bilayers. Macroscopic and single channel conductance experiments showed that ceratotoxin A forms voltage-dependent ion channels in bilayers according to the barrel-stave model. The characteristics of the channel suggest that the C-terminal regions form bundles of five or six helices embedded in the membrane, such that the N-terminal moieties lie on the polar side of the lipid bilayer.

journal_name

Peptides

journal_title

Peptides

authors

Saint N,Marri L,Marchini D,Molle G

doi

10.1016/j.peptides.2003.09.015

subject

Has Abstract

pub_date

2003-11-01 00:00:00

pages

1779-84

issue

11

eissn

0196-9781

issn

1873-5169

pii

S019697810300353X

journal_volume

24

pub_type

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