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A non-zipper-like tetrameric coiled coil promotes membrane fusion

机译：一种非拉链的四聚体卷绕线圈促进膜融合

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Two peptides, Coil-K and Coil-E, form a parallel heterodimeric coiled coil, CC-K/E, and have been shown to promote membrane fusion. This article examines the effects of reversing the sequence of Coil-E (to yield Coil-Er), on coiled-coil formation and membrane fusion. Coiled-coil assembly was studied using circular dichroism spectroscopy, paramagnetic proton NMR, fluorescence spectroscopy, analytical ultracentrifugation and computational simulations. Combined, the data show that Coil-K and Coil-Er combine in a 1?:?1 ratio to form an antiparallel tetramer, reinforcing previous studies that show small changes to peptide sequences strongly affect the stoichiometry and orientation of the resulting assemblies. Cholesterol-modified Coil-K and Coil-Er variants were subsequently tested for their ability to promote membrane fusion and the results were compared to the CC-K/E model system. Surprisingly, no significant differences were found between the two systems, despite the Coil-K/Er complex being ‘non-zipper-like’.
机译：两种肽，线圈-K和线圈-e，形成平行的异二聚体盘绕线圈，CC-K / E，并且已被证明促进膜融合。本文研究了逆转线圈-E（以屈服线圈ER），卷曲线圈形成和膜融合的影响。使用圆形二色光谱，顺磁质子NMR，荧光光谱，分析超速离心和计算模拟研究卷绕线圈组件。组合，数据显示线圈-K和线圈-ER在1？：1的比例以形成反平行的四聚体，增强了对肽序列的小变化的先前研究强烈影响所得组件的化学计量和取向。随后测试胆固醇改性的线圈-K和线圈-ER变体的促进膜融合的能力，并将结果与​​CC-K / E型系统进行比较。令人惊讶的是，两种系统之间没有发现显着的差异，尽管线圈-K / ER复合物是“非拉链”。

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