Protein–protein and protein–lipid interactions in domain-assembly: Lessons from giant unilamellar vesicles
نویسندگان
چکیده
منابع مشابه
Self-assembly of a cholesteryl-modified nucleoside into tubular structures from giant unilamellar vesicles
We recently reported the formation of microand nanometer thick tubules in a binary system of cholesteryl-modified aminouridine and a phosphatidylcholine in aqueous solution upon cooling from 70 C to room temperature (Pescador et al., Chem. Commun, 2010, 46, 5358). To better understand the first steps of the tubular self-assembly and the role of the phospholipid, we investigated now morphologica...
متن کاملTrapping and release of giant unilamellar vesicles in microfluidic wells.
We describe the trapping and release of giant unilamellar vesicles (GUVs) in a thin and wide microfluidic channel, as they cross indentations etched in the channel ceiling. This trapping results from the reduction of the membrane elastic energy, which is stored in the GUV as it squeezes to enter into the thin channel. We demonstrate that GUVs whose diameter is slightly larger than the channel h...
متن کاملLipid domain formation and dynamics in giant unilamellar vesicles explored by fluorescence correlation spectroscopy.
Lipids in eukaryotic cell membranes have been shown to cluster in "rafts" with different lipid/protein compositions and molecular packing. Model membranes such as giant unilamellar vesicles (GUVs) provide a key system to elucidate the physical mechanisms of raft assembly. Despite the large amount of work devoted to the detection and characterization of rafts, one of the most important pieces of...
متن کاملShape and Size of Giant Unilamellar Phospholipid Vesicles Containing Cardiolipin
The effect of cardiolipin content on the shape and size of giant palmitoyloleylphosphatidylcholine/cardiolipin vesicles was studied. Unilamellar vesicles were prepared in sugar solution by the method of electroformation, from mixtures containing up to 50% weight ratio of cardiolipin. At room temperature the vesicles containing cardiolipin exhibited abrupt changes in the curvature of the vesicle...
متن کاملThermodynamic relaxation drives expulsion in giant unilamellar vesicles.
We investigated the thermodynamic relaxation of giant unilamellar vesicles (GUVs) which contained small vesicles within their interior. Quenching these vesicles from their fluid phase (T > T(m)) through the phase transition in the gel state (T < T(m)) drives the inner vesicles to be expelled from the larger mother vesicle via the accompanying decrease in the vesicle area by approximately 25% wh...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 2010
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2010.02.028