scholarly journals Deformation analysis of nonuniform lipid membrane subjected to local inflammations

2021 ◽  
Vol 9 (2) ◽  
pp. 203-229
Author(s):  
Wenhao Yao ◽  
Chun Il Kim
Keyword(s):  
Lipid Membrane ◽  
Deformation Analysis

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.

Deformation Analysis of Box Shape Injection Mouldings in Consideration of Moulding Process.

1993 ◽  
Vol 42 (475) ◽  
pp. 359-363
Author(s):  
Mitomo HIRAI ◽  
Tsuneo HIRAI ◽  
Tsutao KATAYAMA ◽  
Takeshi ISHIKAWA
Keyword(s):  
Deformation Analysis ◽  
Moulding Process

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.

Dimerization of the Antimicrobial Peptide Polyphemusin I into One Polypeptide Chain: Theoretical and Practical Consequences

2019 ◽  
Vol 35 (5) ◽  
pp. 36-41
Author(s):  
V.A. Zenin ◽  
E.G. Sadykhov ◽  
A.N. Fedorov
Keyword(s):  
Antimicrobial Peptides ◽  
Pore Formation ◽  
Lipid Membrane ◽  
Polypeptide Chain ◽  
Unique Identifier ◽  
Bacterial Cultures ◽  
In Series ◽  
The Russian Federation ◽  
Peptide Dimerization ◽  
Putative Mechanism

A strategy of sequential dimerization of monomers of antimicrobial peptides (AMPs) into one polypeptide chain has been implemented on the example of a beta-structural AMP polyphemusin I which is one of the most effective candidate for use as an antibiotic. The possible polyphemusin I monomer and dimer structures in lipid membrane were studied in this work via molecular modeling. To this end, these molecules were chemically synthesized so that the dimer represented two monomers connected in series into one polypeptide chain with a flexible linker. The antimicrobial effects of monomer and dimer were then tested on various bacterial cultures, and their similarity was shown. Therefore, we can conclude that the pore formation is not a putative mechanism of the polyphemusin I action. antimicrobial peptides, peptide dimerization, mechanism of antimicrobial action, polyphemusin The work was supported by the Ministry of Science and Higher Education of the Russian Federation (Project Unique Identifier RFMEFI57517X0151).

Preparation of Chloroplast Lipid Membrane and Lipid-protein Interaction Assay

BIO-PROTOCOL ◽  
2016 ◽  
Vol 6 (3) ◽  
Author(s):  
Kumiko Okazaki ◽  
Shin-ya Miyagishima ◽  
Hajime Wada
Keyword(s):  
Protein Interaction ◽  
Lipid Membrane ◽  
Lipid Protein Interaction
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