pore forming properties of cecropin-melittin hybrid peptide in a natural membrane孔隙形成cecropin-melittin混合肽膜在自然的属性.pdfVIP

Molecules 2009, 14, 5179-5188; doi:10.3390/molecule OPEN ACCESS molecules ISSN 1420-3049 /journal/molecules Article Pore Forming Properties of Cecropin-Melittin Hybrid Peptide in a Natural Membrane Alberto Milani, Mascia Benedusi, Marco Aquila and Giorgio Rispoli * 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; E-Mails: ani@student.unife.it (A.M.); bndmsc@unife.it (M.B.); marco.aquila@student.unife.it (M.A.) * Author to whom correspondence should be addressed; E-Mail: rsg@unife.it; Tel./Fax: +39-0532-455462. 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-CONH ; CM15) were investigated by using 2 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 p