Dynamic light scattering analysis of SNARE-driven membrane fusion and the effects of SNARE-binding flavonoid
- Dynamic light scattering analysis of SNARE-driven membrane fusion and the effects of SNARE-binding flavonoid
- 양유수; 허바울; 공병재; 박준범; 정영훈; 신종혁; 정철현; 권대혁
- SNARE; Membrane fusion; Dynamic light scattering; FRET; Flavonoid
- Issue Date
- Biochemical and biophysical research communications
- VOL 465, NO 4, 864-870
- 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.
- Appears in Collections:
- KIST Publication > Article
- Files in This Item:
There are no files associated with this item.
- RIS (EndNote)
- XLS (Excel)
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.