On the organization of self-assembled actin networks in giant vesicles
| Autor: | M. Bärmann, L. Limozin, Erich Sackmann |
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| Rok vydání: | 2003 |
| Předmět: |
Macromolecular Substances
Membrane Fluidity Polymers Protein Conformation Lipid Bilayers Molecular Conformation Biophysics Nanotechnology macromolecular substances Filamentous actin Polyethylene Glycols Protein filament Materials Testing Fluorescence microscope Membrane fluidity General Materials Science Particle Size Cytoskeleton Actin Persistence length Chemistry Vesicle technology industry and agriculture Surfaces and Interfaces General Chemistry Actins Membrane Liposomes Adsorption Crystallization Dimyristoylphosphatidylcholine Protein Binding Biotechnology |
| Zdroj: | The European Physical Journal E. 10:319-330 |
| ISSN: | 1292-8941 |
| Popis: | We studied the formation of actin scaffolds in giant vesicles of dimyristoylphosphatidylcholine (DMPC). Polymerization of actin was induced at low ionic strength through ionophore-mediated influx of Mg2+ (2 mM). The spatial organization of the filamentous actin was visualized by confocal and epifluorescence microscopy as a function of the filaments length and membrane composition, by including various amounts of cholesterol or lipids with neutral and positively charged polyethyleneglycol headgroups (PEG lipopolymers). In vesicles of pure DMPC, the newly polymerized actin adsorbs to the membrane and forms a thin shell. In the presence of 2.5 mol% lipopolymers or of cholesterol at a molar fraction x=0.37, formation of a thin adsorbed film is impeded. A fuzzy cortex is predominantly formed in vesicles of diameter d smaller than the filament persistence length (d< or =15 microm) while for larger vesicles a homogeneous network formation is favoured in the bulk of the vesicle. The fuzzy-cortex formation is interpreted as a consequence of the reduction of the bending energy if the actin filaments accumulate close to the vesicle wall. |
| Databáze: | OpenAIRE |
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