Ceratotoxins are a-helical cationic peptides isolated from the medfly Ceratitis capitata. These amphipathic peptides were found to display strong antibacterial activity and weak hemolytic activity. When reconstituted into planar lipid bilayers, ceratotoxins developed highly asymmetric I/V curves under voltage ramps and formed, in single-channel experiments, well-defined voltage-dependent ion channels according to the barrel stave model. The antibacterial activity and pore-forming properties of these molecules were well correlated. Similar experiments performed with synthesized truncated fragments showed that the C-terminal domain of ceratotoxins, is strongly implicated in the formation of helical bundles in the membrane whereas the largely cationic N-terminal region is likely to anchor ceratotoxins on the lipid surface.
Bessin, Y., Saint, N., Marri, L., Marchini, D., Molle, G. (2004). Antibacterial activity and pore-forming properties of ceratotoxins: a mechanism of action based on the barrel stave model. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 1667(2), 148-156 [10.1016/j.bbamem.2004.09.011].
Antibacterial activity and pore-forming properties of ceratotoxins: a mechanism of action based on the barrel stave model.
MARRI, LAURA;MARCHINI, DANIELA;
2004-01-01
Abstract
Ceratotoxins are a-helical cationic peptides isolated from the medfly Ceratitis capitata. These amphipathic peptides were found to display strong antibacterial activity and weak hemolytic activity. When reconstituted into planar lipid bilayers, ceratotoxins developed highly asymmetric I/V curves under voltage ramps and formed, in single-channel experiments, well-defined voltage-dependent ion channels according to the barrel stave model. The antibacterial activity and pore-forming properties of these molecules were well correlated. Similar experiments performed with synthesized truncated fragments showed that the C-terminal domain of ceratotoxins, is strongly implicated in the formation of helical bundles in the membrane whereas the largely cationic N-terminal region is likely to anchor ceratotoxins on the lipid surface.File | Dimensione | Formato | |
---|---|---|---|
BBA2004.pdf
non disponibili
Tipologia:
Post-print
Licenza:
NON PUBBLICO - Accesso privato/ristretto
Dimensione
552.63 kB
Formato
Adobe PDF
|
552.63 kB | Adobe PDF | Visualizza/Apri Richiedi una copia |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
https://hdl.handle.net/11365/21206
Attenzione
Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo