scholarly journals Understanding the Dynamics of a Lipid Monolayer on a Water Surface under a Marangoni Flow

2021 ◽  
Vol 5 (2) ◽  
pp. 31
Author(s):  
Yohko F. Yano ◽  
Toshiaki Ina ◽  
Tomoya Uruga
Keyword(s):  
Surface Pressure ◽  
Tilt Angle ◽  
Water Surface ◽  
Biological Membrane ◽  
Translational Motion ◽  
Dynamical Behavior ◽  
Lipid Monolayer ◽  
Marangoni Flow ◽  
X Ray ◽  
Hydrocarbon Chains

Biological membrane is composed of lipid molecules, because of its fluidity, it is possible to carry out physiological functions. Therefore, it is important to study the hydrodynamic properties of membranes toward understanding its function. Here, we observed the dynamical behavior of a lipid monolayer on the water surface under Marangoni flow. By using X-ray reflectometry, we obtained the tilt angle of the hydrocarbon chains of the lipid at different surface pressures. Comparing them with the dynamical surface pressure under Marangoni flow, it was found that the lipid molecules in rotational rather than translational motion. At low surface pressure, the molecular tilt angle is reduced by 20 degrees, even though the molecular area is reduced by at most 10%.

Nanostructure of Fullerene-Bearing Artificial Lipid Monolayer on Water Surface by in Situ X-ray Reflectometry

Langmuir ◽  
2002 ◽  
Vol 18 (25) ◽  
pp. 10042-10045 ◽  
Author(s):  
Emiko Mouri ◽  
Takashi Nakanishi ◽  
Naotoshi Nakashima ◽  
Hideki Matsuoka
Keyword(s):  
Water Surface ◽  
Lipid Monolayer ◽  
X Ray

Direct visualization of phase-separated domains in lipid membranes

1978 ◽  
Vol 36 (2) ◽  
pp. 290-291
Author(s):  
S. W. Hui ◽  
T. P. Stewart
Keyword(s):  
Lipid Membranes ◽  
Structural Information ◽  
Freeze Fracture ◽  
Biological Molecules ◽  
Vacuum Drying ◽  
Direct Visualization ◽  
X Ray Diffraction ◽  
Electron Microscopic ◽  
X Ray ◽  
Hydrocarbon Chains

Direct electron microscopic study of biological molecules has been hampered by such factors as radiation damage, lack of contrast and vacuum drying. In certain cases, however, the difficulties may be overcome by using redundent structural information from repeating units and by various specimen preservation methods. With bilayers of phospholipids in which both the solid and fluid phases co-exist, the ordering of the hydrocarbon chains may be utilized to form diffraction contrast images. Domains of different molecular packings may be recgnizable by placing properly chosen filters in the diffraction plane. These domains would correspond to those observed by freeze fracture, if certain distinctive undulating patterns are associated with certain molecular packing, as suggested by X-ray diffraction studies. By using an environmental stage, we were able to directly observe these domains in bilayers of mixed phospholipids at various temperatures at which their phases change from misible to inmissible states.

Structure of rattlesnake venom lectin determined by single particle high-resolution electron microscopy

1996 ◽  
Vol 54 ◽  
pp. 62-63
Author(s):  
Peter D. Moisiuk ◽  
Daniel R. Beniac ◽  
Ross A. Ridsdale ◽  
Martin Young ◽  
Bhushan Nagar ◽  
...  
Keyword(s):  
High Resolution Electron Microscopy ◽  
Lipid Monolayer ◽  
Outer Diameter ◽  
X Ray Diffraction ◽  
Single Particles ◽  
Crotalus Atrox ◽  
3D Reconstructions ◽  
X Ray ◽  
Rattlesnake Venom ◽  
Covalently Linked

Venom from the rattlesnake Crotalus atrox contains a mixture of enzymes that induce a localized effect leading to hemorrhaging, necrosis and edema. As a member of the crotalid family of snake venoms, Crotalus atrox venom contains a C-type lectin that will agglutinate blood cells in a Ca2+-dependent fashion. The lectin is a hydrophilic protein, consisting of two covalently linked, 135 amino acid residues, identical subunits that are rich in aspartic acid, glutamic acid and lysine. Sequence homology with known carbohydrate recognition domains (CRDs) indicates that rattlesnake venom lectin (RSLV) contains a CRD motif that is not linked to accessory domains. Preliminary X-ray diffraction and sedimentation analysis has indicated that lectin from Crotalus atrox forms decamers composed of two five-fold symmetric pentamers. Single particles of RSVL imaged at – 171°C displayed two distinct orientations on the specimen support (Figure a) following incubation in a crystallization Teflon well, coated with a lipid monolayer consisting of phosphatidylcholine and monosialoganglioside. When lying in an end-on orientation, the lectin exhibited a “pentagonal ring” with an outer diameter of 6.7 nm and an inner hollow core of 1.7 nm. A side orientation was also seen, whereby a thickness of 5.8 nm was measured for the lectin. Image processing of 2280 single particles placed in 100 classes (Figure b) led to 3D reconstructions of RSVL (Figure c). Density limited 3D reconstructions showed the lectin to be made of two five-fold symmetrical rings covalently linked between the five subunits that constitute each ring of this homodimer. These results are consistent with sedimentation and preliminary X-ray diffraction analysis on the shape of RSVL and provide the framework for structural verification by 2D electron crystallography.

scholarly journals Curvature Elastic Properties of Phosphatidylethanolamines with Mono-and Polyunsaturated Hydrocarbon Chains - An NMR and X-Ray Diffraction Study

2012 ◽  
Vol 102 (3) ◽  
pp. 413a
Author(s):  
Walter E. Teague ◽  
Olivier Soubias ◽  
Nola L. Fuller ◽  
R. Peter Rand ◽  
Klaus Gawrisch
Keyword(s):  
Diffraction Study ◽  
Elastic Properties ◽  
X Ray Diffraction ◽  
X Ray ◽  
Hydrocarbon Chains

Nanostructure of a Photochromic Polymer/Liquid Crystal Hybrid Monolayer on a Water Surface Observed by in Situ X-ray Reflectometry

Langmuir ◽  
2002 ◽  
Vol 18 (10) ◽  
pp. 3875-3879 ◽  
Author(s):  
Keitaro Kago ◽  
Takahiro Seki ◽  
Randolf R. Schücke ◽  
Emiko Mouri ◽  
Hideki Matsuoka ◽  
...  
Keyword(s):  
Liquid Crystal ◽  
Water Surface ◽  
Polymer Liquid ◽  
X Ray ◽  
Photochromic Polymer ◽  
Polymer Liquid Crystal

scholarly journals Diffracting-grain identification from electron backscatter diffraction maps during residual stress measurements: a comparison between the sin2ψ and cosα methods

2019 ◽  
Vol 52 (4) ◽  
pp. 828-843 ◽  
Author(s):  
Dorian Delbergue ◽  
Damien Texier ◽  
Martin Lévesque ◽  
Philippe Bocher
Keyword(s):  
Residual Stress ◽  
Grain Size ◽  
Tilt Angle ◽  
Measurement Errors ◽  
Electron Backscatter Diffraction ◽  
Measurement Techniques ◽  
Single Exposure ◽  
X Ray ◽  
Electron Backscatter ◽  
Backscatter Diffraction

X-ray diffraction (XRD) is a widely used technique to evaluate residual stresses in crystalline materials. Several XRD measurement methods are available. (i) The sin2ψ method, a multiple-exposure technique, uses linear detectors to capture intercepts of the Debye–Scherrer rings, losing the major portion of the diffracting signal. (ii) The cosα method, thanks to the development of compact 2D detectors allowing the entire Debye–Scherrer ring to be captured in a single exposure, is an alternative method for residual stress measurement. The present article compares the two calculation methods in a new manner, by looking at the possible measurement errors related to each method. To this end, sets of grains in diffraction condition were first identified from electron backscatter diffraction (EBSD) mapping of Inconel 718 samples for each XRD calculation method and its associated detector, as each method provides different sets owing to the detector geometry or to the method specificities (such as tilt-angle number or Debye–Scherrer ring division). The X-ray elastic constant (XEC) ½S 2, calculated from EBSD maps for the {311} lattice planes, was determined and compared for the different sets of diffracting grains. It was observed that the 2D detector captures 1.5 times more grains in a single exposure (one tilt angle) than the linear detectors for nine tilt angles. Different XEC mean values were found for the sets of grains from the two XRD techniques/detectors. Grain-size effects were simulated, as well as detector oscillations to overcome them. A bimodal grain-size distribution effect and `artificial' textures introduced by XRD measurement techniques are also discussed.

Lipolytic activity of ricin from Ricinus sanguineus and Ricinus communis on neutral lipids

2001 ◽  
Vol 358 (3) ◽  
pp. 773-781 ◽  
Author(s):  
Sophie LOMBARD ◽  
Mohamed E. HELMY ◽  
Gérard PIÉRONI
Keyword(s):  
Surface Pressure ◽  
Specific Activity ◽  
Neutral Lipids ◽  
Ricinus Communis ◽  
Lipolytic Activity ◽  
Fatty Acid Esters ◽  
Lipid Monolayer ◽  
Serine Esterase ◽  
Order Of Magnitude ◽  
Esterase Inhibitor

The present study was carried out with a view of determining ricin lipolytic activity on neutral lipids in emulsion and in a membrane-like model. Using 2,3-dimercapto-1-propanol tributyrate (BAL-TC4) as substrate, the lipolytic activity of ricin was found to be proportional to ricin and substrate concentrations, with an apparent Km (Km,app) of 2.4mM, a kcat of 200min−1 and a specific activity of 1.0unit/mg of protein. This work was extended to p-nitrophenyl (pNP) fatty acid esters containing two to twelve carbon atoms. Maximum lipolytic activity was registered on pNP decanoate (pNPC10), with a Km,app of 3.5mM, a kcat of 173min−1 and a specific activity of 3.5units/mg of protein. Ricin lipolytic activity is pH and galactose dependent, with a maximum at pH7.0 in the presence of 0.2M galactose. Using the monolayer technique with dicaprin as substrate, ricin showed a lipolytic activity proportional to the ricin concentration at 20mN/m, which is dependent on the surface pressure of the lipid monolayer and is detectable up to 30mN/m, a surface pressure that is of the same order of magnitude as that of natural cell membranes. The methods based on pNPC10 and BAL-TC4 hydrolysis are simple and reproducible; thus they can be used for routine studies of ricin lipolytic activity. Ricin from Ricinus communis and R. sanguineus were treated with diethyl p-nitrophenylphosphate, an irreversible serine esterase inhibitor, and their lipolytic activities on BAL-TC4 and pNPC10, and cytotoxic activity, were concurrently recorded. A reduction in lipolytic activity was accompanied by a decrease in cytotoxicity on Caco2 cells. These data support the idea that the lipolytic activity associated with ricin is relevant to a lipase whose activity is pH and galactose dependent, sensitive to diethyl p-nitrophenylphosphate, and that a lipolytic step may be involved in the process of cell poisoning by ricin. Both colorimetric tests used in this study are sensitive enough to be helpful in the detection of possible lipolytic activities associated with other cytotoxins or lectins.

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