Dynamic light scattering analysis of SNARE-driven membrane fusion and the effects of SNARE-binding flavonoid

Title
Dynamic light scattering analysis of SNARE-driven membrane fusion and the effects of SNARE-binding flavonoid
Authors
양유수허바울공병재박준범정영훈신종혁정철현권대혁
Keywords
SNARE; Membrane fusion; Dynamic light scattering; FRET; Flavonoid
Issue Date
2015-10
Publisher
Biochemical and biophysical research communications
Citation
VOL 465, NO 4, 864-870
Abstract
Soluble N-ethylmaleimide-sensitive-factor attachment protein receptor (SNARE) proteins generate energy required for membrane fusion. They form a parallelly aligned four-helix bundle called the SNARE complex, whose formation is initiated from the N terminus and proceeds toward the membraneproximal C terminus. Previously, we have shown that this zippering-like process can be controlled by several flavonoids that bind to the intermediate structures formed during the SNARE zippering. Here, our aim was to test whether the fluorescence resonance energy transfer signals that are observed during the inner leaflet mixing assay indeed represent the hemifused vesicles. We show that changes in vesicle size accompanying the merging of bilayers is a good measure of progression of the membrane fusion. Two merging vesicles with the same size D in diameter exhibited their hydrodynamic diameters 2D þ d (d, intermembrane distance), 2D and ffiffiffi 2 p D as membrane fusion progressed from vesicle docking to hemifusion and full fusion, respectively. A dynamic light scattering assay of membrane fusion suggested that myricetin stopped membrane fusion at the hemifusion state, whereas delphinidin and cyanidin prevented the docking of the vesicles. These results are consistent with our previous findings in fluorescence resonance energy transfer assays.
URI
http://pubs.kist.re.kr/handle/201004/50251
ISSN
0006291X
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KIST Publication > Article
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