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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

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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 which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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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