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

Yamamoto, Akihisa; Tanaka, Motomu; Abuillan, Wasim; Körner, Alexander; Burk, Alexandra S.; Ries, Annika; Werz, Daniel B.; Demé, Bruno

doi:10.1063/1.4918585

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

Full Record
Other Related Research

Abstract

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.

Authors:

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

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

Publication Date:: Tue Apr 21 00:00:00 EDT 2015

OSTI Identifier:: 22416238

Resource Type:: Journal Article

Journal Name:: Journal of Chemical Physics

Additional Journal Information:: Journal Volume: 142; Journal Issue: 15; Other Information: (c) 2015 Author(s); Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0021-9606

Country of Publication:: United States

Language:: English

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

Citation Formats


                    Yamamoto, Akihisa, Tanaka, Motomu, Institute for Integrated Cell-Material Sciences, Abuillan, Wasim, Körner, Alexander, Burk, Alexandra S., Institute of Toxicology and Genetics, Karlsruhe Institute of Technology, 76021 Karlsruhe, Ries, Annika, Werz, Daniel B., and Demé, Bruno. Influence of length and conformation of saccharide head groups on the mechanics of glycolipid membranes: Unraveled by off-specular neutron scattering.  United States: N. p., 2015. 
        Web.  doi:10.1063/1.4918585.

Copy to clipboard


                    Yamamoto, Akihisa, Tanaka, Motomu, Institute for Integrated Cell-Material Sciences, Abuillan, Wasim, Körner, Alexander, Burk, Alexandra S., Institute of Toxicology and Genetics, Karlsruhe Institute of Technology, 76021 Karlsruhe, Ries, Annika, Werz, Daniel B., & Demé, Bruno. Influence of length and conformation of saccharide head groups on the mechanics of glycolipid membranes: Unraveled by off-specular neutron scattering.  United States.  https://doi.org/10.1063/1.4918585

Copy to clipboard


                    Yamamoto, Akihisa, Tanaka, Motomu, Institute for Integrated Cell-Material Sciences, Abuillan, Wasim, Körner, Alexander, Burk, Alexandra S., Institute of Toxicology and Genetics, Karlsruhe Institute of Technology, 76021 Karlsruhe, Ries, Annika, Werz, Daniel B., and Demé, Bruno. 2015.  
        "Influence of length and conformation of saccharide head groups on the mechanics of glycolipid membranes: Unraveled by off-specular neutron scattering".  United States.  https://doi.org/10.1063/1.4918585.

Copy to clipboard


                    
@article{osti_22416238,

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

  author       = {Yamamoto, Akihisa and Tanaka, Motomu and Institute for Integrated Cell-Material Sciences and Abuillan, Wasim and Körner, Alexander and Burk, Alexandra S. and Institute of Toxicology and Genetics, Karlsruhe Institute of Technology, 76021 Karlsruhe and Ries, Annika and Werz, Daniel B. and Demé, Bruno},

  abstractNote = {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.},

  doi          = {10.1063/1.4918585},

  url          = {https://www.osti.gov/biblio/22416238},
  journal      = {Journal of Chemical Physics},

  issn         = {0021-9606},

  number       = 15,

  volume       = 142,

  place        = {United States},

  year         = {Tue Apr 21 00:00:00 EDT 2015},

  month        = {Tue Apr 21 00:00:00 EDT 2015}

}

Copy to clipboard

Journal Article:

https://doi.org/10.1063/1.4918585

Other availability

Find in Google Scholar

Search WorldCat to find libraries that may hold this journal

Save / Share:

Export Metadata

Save to My Library

Similar records in OSTI.GOV collections:

Structural Determination and Tryptophan Fluorescence of Heterokaryon Incompatibility C2 Protein (HET-C2), a Fungal Glycolipid Transfer Protein (GLTP), Provide Novel Insights into Glycolipid Specificity and Membrane Interaction by the GLTP Fold

Journal Article Kenoth, Roopa; Simanshu, Dhirendra; Kamlekar, Ravi; ... - J. Biol. Chem.

HET-C2 is a fungal protein that transfers glycosphingolipids between membranes and has limited sequence homology with human glycolipid transfer protein (GLTP). The human GLTP fold is unique among lipid binding/transfer proteins, defining the GLTP superfamily. Herein, GLTP fold formation by HET-C2, its glycolipid transfer specificity, and the functional role(s) of its two Trp residues have been investigated. X-ray diffraction (1.9 {angstrom}) revealed a GLTP fold with all key sugar headgroup recognition residues (Asp{sup 66}, Asn{sup 70}, Lys{sup 73}, Trp{sup 109}, and His{sup 147}) conserved and properly oriented for glycolipid binding. Far-UV CD showed secondary structure dominated by {alpha}-helices and amore »« less
https://doi.org/10.1074/jbc.M109.093203
CHARMM-GUI Membrane Builder for Complex Biological Membrane Simulations with Glycolipids and Lipoglycans

Journal Article Lee, Jumin; Patel, Dhilon; Stahle, Jonas; ... - Journal of Chemical Theory and Computation

Glycolipids (such as glycoglycerolipids, glycosphingolipids, and glycosylphosphatidylinositol) and lipoglycans (such as lipopolysaccharides (LPS), lipooligosaccharides (LOS), mycobacterial lipoarabinomannan, and mycoplasma lipoglycans) are typically found on the surface of cell membranes and play crucial roles in various cellular functions. Characterizing their structure and dynamics at the molecular level is essential to understand their biological roles, but systematic generation of glycolipid and lipoglycan structures is challenging because of great variations in lipid structures and glycan sequences (i.e., carbohydrate types and their linkages). To facilitate the generation of all-atom glycolipid/LPS/LOS structures, we have developed Glycolipid Modeler and LPS Modeler in CHARMM-GUI (http://www.charmm-gui.org), a web-basedmore »« less
https://doi.org/10.1021/acs.jctc.8b01066
Mechanical properties of interacting lipopolysaccharide membranes from bacteria mutants studied by specular and off-specular neutron scattering

Journal Article Schneck, Emanuel; Tanaka, Motomu; Oliveira, Rafael; ... - Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics (Print)

Specular and off-specular neutron scattering are used to study the influence of molecular chemistry (mutation) on the intermembrane interactions and mechanical properties of the outer membrane of Gram-negative bacteria consisting of lipopolysaccharides (LPSs). For this purpose, solid-supported multilayers of mutant LPS membranes are deposited on silicon wafers and hydrated either at defined humidity or in bulk buffers. The planar sample geometry allows to identify out-of-plane and in-plane scattering vector components. The measured two-dimensional reciprocal space maps are simulated with membrane displacement correlation functions determined by two mechanical parameters (vertical compression modulus and bending rigidity) and an effective cutoff radius formore »« less
https://doi.org/10.1103/PHYSREVE.80.041929
Mechanism of glucocerebrosidase activation and dysfunction in Gaucher disease unraveled by molecular dynamics and deep learning

Journal Article Romero, Raquel; Ramanathan, Arvind; Yuen, Tony; ... - Proceedings of the National Academy of Sciences of the United States of America

The lysosomal enzyme glucocerebrosidase-1 (GCase) catalyzes the cleavage of a major glycolipid glucosylceramide into glucose and ceramide. The absence of fully functional GCase leads to the accumulation of its lipid substrates in lysosomes, causing Gaucher disease, an autosomal recessive disorder that displays profound genotype–phenotype nonconcordance. More than 250 disease-causing mutations inGBA1, the gene encoding GCase, have been discovered, although only one of these, N370S, causes 70% of disease. In this work, we have used a knowledge-based docking protocol that considers experimental data of protein–protein binding to generate a complex between GCase and its known facilitator protein saposin C (SAPC). Multiscalemore »« less
Cited by 37
https://doi.org/10.1073/pnas.1818411116

Full Text Available
Characterization of glycolipid galactosyltransferases from embryonic chicken brain

Thesis/Dissertation Kyle, J

Glycolipid galactosyltransferases (GalT-3 and GalT-4) were solubilized from a membrane fraction isolated from embryonic chicken brain. The profiles of specific activity and total units per brain of GalT-3 and GalT-4 varied with embryonic age. GalT-4 had the highest specific activity at 9 days of embryonic development and showed a steady decrease until hatching. GalT-3 showed a gradual increase in specific activity. Both GalT3 and GalT-4 showed a steady increase in total units per brain throughout embryonic development. The solubilized enzymes could be separated using gel filtration, ion exchange chromatography or affinity chromatography on ..cap alpha..-lactalbumin-agarose. Data obtained in the studymore »« less

Similar Records