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Pore Forming Properties of Cecropin-Melittin Hybrid Peptide in a Natural Membrane
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; in revised form: 4 December 2009 / Accepted: 10 December 2009 / Published: 11 December 2009
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
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MDPI and ACS Style
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.
Milani A, Benedusi M, Aquila M, Rispoli G. Pore Forming Properties of Cecropin-Melittin Hybrid Peptide in a Natural Membrane. Molecules. 2009; 14(12):5179-5188.
Milani, Alberto; Benedusi, Mascia; Aquila, Marco; Rispoli, Giorgio. 2009. "Pore Forming Properties of Cecropin-Melittin Hybrid Peptide in a Natural Membrane." Molecules 14, no. 12: 5179-5188.