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.
Molecules. 2009 Dec 11;14(12):5179-88. doi: 10.3390/molecules14125179.
The pore forming properties of synthetic cecropin-melittin hybrid peptide (Acetyl-KWKLFKKIGAVLKVL-CONH(2); 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 approximately 50 ms with a computer-controlled microperfusion system. Once the main OS endogenous conductance was blocked with light, the OS membrane resistance was >or=1 G Omega, 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.
采用全细胞膜片钳技术的细胞贴附式记录，从蛙眼视网膜中分离出光感受器视杆外段（OS），研究了合成抗菌肽 Cecropin-Melittin 杂合肽（Acetyl-KWKLFKKIGAVLKVL-CONH2；CM15）的成孔特性。计算机控制的微灌注系统将 CM15 在大约 50 毫秒内应用（和去除）于 OS。一旦用光阻断主要 OS 内源性电导，OS 膜电阻就会大于或等于 1 GΩ，从而可以进行高分辨率、低噪声记录。与 Alamethicines 不同，CM15 产生电压非依赖性的膜通透性，重复应用肽导致通透性逐渐增加，并且在低肽浓度下未检测到单通道事件。总的来说，这些结果表明 CM15 通过环形机制形成孔。
