Effects of Alkali Cations and Halide Anions on the DOPC Lipid Membrane†

2009 ◽  
Vol 113 (26) ◽  
pp. 7235-7243 ◽  
Author(s):  
Robert Vácha ◽  
Shirley W. I. Siu ◽  
Michal Petrov ◽  
Rainer A. Böckmann ◽  
Justyna Barucha-Kraszewska ◽  
...  
Keyword(s):  
Lipid Membrane ◽  
Alkali Cations ◽  
Halide Anions

Effects of Alkali Cations and Halide Anions on the Self-Assembly of Phosphatidylcholine in Oils

Langmuir ◽  
2016 ◽  
Vol 32 (46) ◽  
pp. 12166-12174 ◽  
Author(s):  
Shih-Ting Lin ◽  
Chen-Shin Lin ◽  
Ya-Ying Chang ◽  
Andrew E. Whitten ◽  
Anna Sokolova ◽  
...  
Keyword(s):  
Self Assembly ◽  
The Self ◽  
Alkali Cations ◽  
Halide Anions

Corrections in the CHARMM36 Parametrization of Chloride Interactions with Proteins, Lipids, and Alkali Cations, and Extension to Other Halide Anions

2021 ◽  
Author(s):  
Esam A. Orabi ◽  
Tuǧba N. Öztürk ◽  
Nathan Bernhardt ◽  
José D. Faraldo-Gómez
Keyword(s):  
Alkali Cations ◽  
Halide Anions

Chapter 2b: The molecular antigenic structure of the TBEV

2020 ◽  
Keyword(s):  
Conformational Changes ◽  
Neutralizing Antibodies ◽  
Lipid Membrane ◽  
Cell Entry ◽  
Antigenic Structure ◽  
E Proteins ◽  
Amino Acid Sequence Level ◽  
Endosomal Membrane ◽  
E Protein ◽  
Golgi Network

TBEV-particles are assembled in an immature, noninfectious form in the endoplasmic reticulum by the envelopment of the viral core (containing the viral RNA) by a lipid membrane associated with two viral proteins, prM and E. Immature particles are transported through the cellular exocytic pathway and conformational changes induced by acidic pH in the trans-Golgi network allow the proteolytic cleavage of prM by furin, a cellular protease, resulting in the release of mature and infectious TBE-virions. The E protein controls cell entry by mediating attachment to as yet ill-defined receptors as well as by low-pH-triggered fusion of the viral and endosomal membrane after uptake by receptor-mediated endocytosis. Because of its key functions in cell entry, the E protein is the primary target of virus neutralizing antibodies, which inhibit these functions by different mechanisms. Although all flavivirus E proteins have a similar overall structure, divergence at the amino acid sequence level is up to 60 percent (e.g. between TBE and dengue viruses), and therefore cross-neutralization as well as (some degree of) cross-protection are limited to relatively closely related flaviviruses, such as those constituting the tick-borne encephalitis serocomplex.

Electrophysiological Characterization of Transport Across Outer Membrane Channels from Gram-Negative Bacteria in Their Native Environment

2019 ◽  
Author(s):  
Jiajun Wang ◽  
Rémi Terrasse ◽  
Jayesh Arun Bafna ◽  
Lorraine Benier ◽  
Mathias Winterhalter
Keyword(s):  
Outer Membrane ◽  
Lipid Membrane ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Multi Drug Resistance ◽  
Gram Negative Bacteria ◽  
Membrane Channels ◽  
Gram Negative ◽  
Electrophysiological Characterization

Multi-drug resistance in Gram-negative bacteria is often associated with low permeability of the outer membrane. To investigate the role of membrane channels in the uptake of antibiotics, we extract, purify and reconstitute them into artificial planar membranes. To avoid this time-consuming procedure, here we show a robust approach using fusion of native outer membrane vesicles (OMV) into planar lipid bilayer which moreover allows also to some extend the characterization of membrane protein channels in their native environment. Two major membrane channels from <i>Escherichia coli</i>, OmpF and OmpC, were overexpressed from the host and the corresponding OMVs were collected. Each OMV fusion revealed surprisingly single or only few channel activities. The asymmetry of the OMV´s translates after fusion into the lipid membrane with the LPS dominantly present at the side of OMV addition. Compared to conventional reconstitution methods, the channels fused from OMVs containing LPS have similar conductance but a much broader distribution. The addition of Enrofloxacin on the LPS side yields somewhat higher association (<i>k<sub>on</sub></i>) and lower dissociation (<i>k<sub>off</sub></i>) rates compared to LPS-free reconstitution. We conclude that using outer membrane vesicles is a fast and easy approach for functional and structural studies of membrane channels in the native membrane.

Capacitance extraction method for a free-standing bilayer lipid membrane formed over an aperture in a nanofabricated silicon chip

2020 ◽  
Vol 59 (SI) ◽  
pp. SIIK02
Author(s):  
Yasutaka Tomioka ◽  
Shogo Takashima ◽  
Masataka Moriya ◽  
Hiroshi Shimada ◽  
Fumihiko Hirose ◽  
...  
Keyword(s):  
Extraction Method ◽  
Lipid Membrane ◽  
Bilayer Lipid Membrane ◽  
Free Standing ◽  
Capacitance Extraction ◽  
Bilayer Lipid

Phase Transitions in Phospholipid Monolayers Studied by Atomic Force Microscopy and Langmuir-Blodgett Technique

2008 ◽  
Vol 59 (11) ◽  
Author(s):  
Maria Tomoaia-Cotisel ◽  
Aurora Mocanu
Keyword(s):  
Atomic Force Microscopy ◽  
Lipid Membrane ◽  
Phase Behaviour ◽  
Membrane Interface ◽  
Force Microscopy ◽  
Langmuir Blodgett ◽  
Atomic Force ◽  
Phospholipid Monolayers ◽  
Air Water Interface ◽  
Condensed Liquid

The phase behaviour and surface structure of dipalmitoyl phosphatidyl choline (DPPC) monolayers at the air/water interface, in the absence and the presence of procaine, have been investigated by Langmuir-Blodgett (LB) technique and atomic force microscopy. The LB films were transferred on mica, at a controlled surface pressure, characteristic for the expanded liquid to condensed liquid phase transition of pure DPPC monolayers. The results indicate that procaine penetrates into and specifically interacts with phospholipid monolayers stabilizing the lipid membrane interface.

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