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

作者：Zheng Tingting; Bulacu Monica; Daudey Geert; Versluis Frank; Voskuhl Jens; Martelli Giuliana; Raap Jan; Sevink G J Agur; Kros Alexander^*; Boyle Aimee L^*

来源：RSC Advances, 2016, 6(10): 7990-7998.

DOI：10.1039/c5ra26175a

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'.

• 出版日期2016