ArticleThe European physical journal. E, Soft matter2011
Synaptic vesicles studied by dynamic light scattering.
Article in The European physical journal. E, Soft matter, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Neurotransmitter uptake of synaptic vesicles studied by X-ray diffraction.European biophysics journal : EBJ · 2022Article
- Membrane fusion studied by colloidal probes.European biophysics journal : EBJ · 2021Review
- Vesicle Adhesion and Fusion Studied by Small-Angle X-Ray Scattering.Biophysical journal · 2018Article
- Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.Nature communications · 2015Article
- Qualitative and quantitative characterization of protein-phosphoinositide interactions with liposome-based methods.Autophagy · 2013Article
- Coiled-coil formation on lipid bilayers--implications for docking and fusion efficiency.Biophysical journal · 2012Article
- Membrane fusion intermediates via directional and full assembly of the SNARE complex.Science (New York, N.Y.) · 2012Article
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Authors and funding
6 authors.
Funding
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Abstract
The size polydispersity distribution of synaptic vesicles (SVs) is characterized under quasi-physiological conditions by dynamic light scattering (DLS). Highly purified fractions of SVs obtained from rat brain still contain a small amount of larger contaminant structures, which can be quantified by DLS and further reduced by asymmetric-flow field-flow (AFFF) fractionation. The intensity autocorrelation functions g (2)(τ) recorded from these samples are analyzed by a constrained regularization method as well as by an alternative direct modeling approach. The results are in quantitative agreement with the polydispersity obtained from cryogenic electron microscopy of vitrified SVs. Next, different vesicle fusion assays based on samples composed of SVs and small unilamellar proteoliposomes with the fusion proteins syntaxin 1 and SNAP-25A are characterized by DLS. The size increase of the proteoliposomes due to SNARE-dependent fusion with SVs is quantified by DLS under quasi-physiological conditions.
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Registered trials
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