Influence of length and conformation of saccharide head groups on the mechanics of glycolipid membranes: Unraveled by off-specular neutron scattering

Journal Article · Tue Apr 21 00:00:00 EDT 2015 · Journal of Chemical Physics

DOI:https://doi.org/10.1063/1.4918585· OSTI ID:22416238

Yamamoto, Akihisa; Tanaka, Motomu ^[1]; Abuillan, Wasim; Körner, Alexander ^[1]; Burk, Alexandra S. ^[1]; Ries, Annika ^[2]; Werz, Daniel B. ^[3]; Demé, Bruno ^[4]

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1. Physical Chemistry of Biosystems, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg (Germany)
2. Institute of Organic and Biomolecular Chemistry, University of Göttingen, 37077 Göttingen (Germany)
3. Institute of Organic Chemistry, Technische Universität Braunschweig, 38106 Braunschweig (Germany)
4. Institut Laue-Langevin, 38042 Grenoble Cedex 9, Grenoble (France)

The mechanical properties of multilayer stacks of Gb3 glycolipid that play key roles in metabolic disorders (Fabry disease) were determined quantitatively by using specular and off-specular neutron scattering. Because of the geometry of membrane stacks deposited on planar substrates, the scattered intensity profile was analyzed in a 2D reciprocal space map as a function of in-plane and out-of-plane scattering vector components. The two principal mechanical parameters of the membranes, namely, bending rigidity and compression modulus, can be quantified by full calculation of scattering functions with the aid of an effective cut-off radius that takes the finite sample size into consideration. The bulkier “bent” Gb3 trisaccharide group makes the membrane mechanics distinctly different from cylindrical disaccharide (lactose) head groups and shorter “bent” disaccharide (gentiobiose) head groups. The mechanical characterization of membranes enriched with complex glycolipids has high importance in understanding the mechanisms of diseases such as sphingolipidoses caused by the accumulation of non-degenerated glycosphingolipids in lysosomes or inhibition of protein synthesis triggered by the specific binding of Shiga toxin to Gb3.

• OSTI ID: 22416238
• Journal Information: Journal of Chemical Physics, Vol. 142, Issue 15; Other Information: (c) 2015 Author(s); Country of input: International Atomic Energy Agency (IAEA); ISSN 0021-9606
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
COMPRESSION
GLYCOLIPIDS
LACTOSE
LAYERS
LYSOSOMES
MECHANICAL PROPERTIES
MEMBRANES
NEUTRON DIFFRACTION
PROTEINS
STACKS
SUBSTRATES
SYNTHESIS
TOXINS
VECTORS