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Molecules 2009, 14(12), 5179-5188; doi:10.3390/molecules14125179
Article

Pore Forming Properties of Cecropin-Melittin Hybrid Peptide in a Natural Membrane

,
,
 and
*
Dipartimento di Biologia ed Evoluzione, Sezione di Fisiologia e Biofisica, National Institute of Neuroscience and Neuroscience Center, Università di Ferrara, Via L. Borsari 46, I-44100 Ferrara, Italy
* Author to whom correspondence should be addressed.
Received: 2 November 2009 / Revised: 4 December 2009 / Accepted: 10 December 2009 / Published: 11 December 2009
(This article belongs to the Special Issue Molecular Diversity Feature Papers)
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Abstract

The pore forming properties of synthetic cecropin-melittin hybrid peptide (Acetyl-KWKLFKKIGAVLKVL-CONH2; CM15) were investigated by using photoreceptor rod outer segments (OS) isolated from frog retinae obtained by using the whole-cell configuration of the patch-clamp technique. CM15 was applied (and removed) to (from) the OS in ~50 ms with a computer-controlled microperfusion system. Once the main OS endogenous conductance was blocked with light, the OS membrane resistance was ≥1 GΩ, allowing high resolution, low-noise recordings. Different to alamethicines, CM15 produced voltage-independent membrane permeabilisation, repetitive peptide application caused a progressive permeabilisation increase, and no single-channel events were detected at low peptide concentrations. Collectively, these results indicate a toroidal mechanism of pore formation by CM15.
Keywords: peptide antibiotics; pore-forming toxins; photoreceptors; ion channels; patch clamp peptide antibiotics; pore-forming toxins; photoreceptors; ion channels; patch clamp
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).
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Milani, A.; Benedusi, M.; Aquila, M.; Rispoli, G. Pore Forming Properties of Cecropin-Melittin Hybrid Peptide in a Natural Membrane. Molecules 2009, 14, 5179-5188.

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