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Determination of Asymmetric Structure of Ganglioside-DPPC Mixed Vesicle Using SANS, SAXS, and DLS

Mitsuhiro Hirai ^*, Hiroki Iwase , Tomohiro Hayakawa ^*, Masaharu Koizumi ^* and Hiroshi Takahashi ^*

^* Department of Physics, Gunma University, Maebashi 371-8510, Japan; and Institute of Materials Structure Science, KEK, 1-1 Oho, Tsukuba 305-0801, Japan

Correspondence: Address reprint requests to Mitsuhiro Hirai, Dept. of Physics, Gunma University 4-2 Aramaki, Maebashi 371-8510, Japan. Tel.: +81-272-20-7554; Fax: +81-272-20-7551 or 7552, E-mail: mhirai{at}fs.aramaki.gunma-u.ac.jp.

Functions of mammalian cell membrane microdomains being rich in glycosphingolipids, so-called rafts, are now one of the current hot topics in cell biology from the intimate relation to cell adhesion and signaling. However, little is known about the role of glycosphingolipids in the formation and stability of the domains. By the use of the inverse contrast variation method in small-angle neutron scattering (SANS), combined with small-angle x-ray scattering (SAXS) and dynamic light scattering (DLS), we have determined an asymmetric internal structure of the bilayer of the small unilamellar vesicle (SUV) of monosialoganglioside (G_M1)-dipalmitoylphosphatidylcholine (DPPC) mixture ([G_M1]:[DPPC] = 0.1:1). A direct method using a shell-model fitting with a size distribution function describes consistently all experimental results of SANS, SAXS, and DLS. We have found that G_M1 molecules predominantly localize at SUV outer surface to form a highly hydrophilic layer which is dehydrated with the rise of temperature from 25°C to 55°C accompanied by the conformational change of the oligosaccharide chains. The average SUV size determined is 200 Å, which is comparable to the reported value 260 ± 130 Å of glycosphingolipids microdomains. The present results suggest that the preferential asymmetric distribution of gangliosides is essential to define the size and stability of the domains.

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