scholarly journals The lipid bilayer membrane and its protein constituents

2018 ◽  
Vol 150 (11) ◽  
pp. 1472-1483 ◽  
Author(s):  
Janice L. Robertson
Keyword(s):  
Membrane Proteins ◽  
Cell Membrane ◽  
Lipid Bilayer ◽  
Lipid Bilayers ◽  
External Solution ◽  
Bilayer Membrane ◽  
Lipid Bilayer Membrane ◽  
General Physiology ◽  
Selective Permeability ◽  
Solvent Environment

In 1918, the year the Journal of General Physiology was founded, there was little understanding of the structure of the cell membrane. It was evident that cells had invisible barriers separating the cytoplasm from the external solution. However, it would take decades before lipid bilayers were identified as the essential constituent of membranes. It would take even longer before it was accepted that there existed hydrophobic proteins that were embedded within the membrane and that these proteins were responsible for selective permeability in cells. With a combination of intuitive experiments and quantitative thinking, the last century of cell membrane research has led us to a molecular understanding of the structure of the membrane, as well as many of the proteins embedded within. Now, research is turning toward a physical understanding of the reactions of membrane proteins and lipids in this unique and incredibly complex solvent environment.

Ligand-Decoration Determines the Translational and Rotational Dynamics of Nanoparticles on a Lipid Bilayer Membrane

2021 ◽  
Author(s):  
Zhihong Zhang ◽  
Wendong Ma ◽  
Kejie He ◽  
Bing Yuan ◽  
Kai Yang
Keyword(s):  
Cell Membrane ◽  
Lipid Bilayer ◽  
Bilayer Membrane ◽  
Rotational Dynamics ◽  
Lipid Bilayer Membrane ◽  
Membrane Interactions ◽  
Therapeutic Applications ◽  
Underlying Mechanisms

Nanoparticles (NPs) promise a huge potential for clinically diagnostic and therapeutic applications. However, the nano-bio (e.g., the NP-cell membrane) interactions and underlying mechanisms are still largely elusive. In this work,...

Aqueous-filled polymer microcavity arrays: versatile & stable lipid bilayer platforms offering high lateral mobility to incorporated membrane proteins

The Analyst ◽  
2015 ◽  
Vol 140 (9) ◽  
pp. 3012-3018 ◽  
Author(s):  
Hajra Basit ◽  
Vinnie Gaul ◽  
Sean Maher ◽  
Robert J. Forster ◽  
Tia E. Keyes
Keyword(s):  
Membrane Proteins ◽  
Cell Membrane ◽  
Lipid Bilayer ◽  
Lipid Bilayers ◽  
Membrane Model ◽  
Lateral Mobility ◽  
Spherical Cap ◽  
Filled Polymer ◽  
Cell Membrane Model

A robust new supported cell membrane model is described comprising lipid bilayers supported on aqueous filled spherical cap pores in PDMS, both lipid and reconstituted membrane proteins diffuse unhindered by the underlying support.

Supported lipid bilayer membrane arrays on micro-patterned ITO electrodes

RSC Advances ◽  
2016 ◽  
Vol 6 (76) ◽  
pp. 72821-72826 ◽  
Author(s):  
Xuejing Wang ◽  
Ying Zhang ◽  
Hongmei Bi ◽  
Xiaojun Han
Keyword(s):  
Cell Membrane ◽  
Fluorescence Microscopy ◽  
Lipid Bilayer ◽  
Electrochemical Detection ◽  
Bilayer Membrane ◽  
Lipid Bilayer Membrane ◽  
Biophysical Properties ◽  
Supported Lipid Bilayer ◽  
Array Platform ◽  
Lipid Bilayer Arrays

Lipid bilayer arrays were formed on micropatterned ITO electrodes. With this bilayer array platform both the fluorescence microscopy and electrochemical detection can be realized to explore the biophysical properties of cell membrane.

scholarly journals Transmembrane signal transduction by cofactor transport

2021 ◽  
Author(s):  
Istvan Kocsis ◽  
Yudi Ding ◽  
Nicholas H. Williams ◽  
Christopher A. Hunter
Keyword(s):  
Signal Transduction ◽  
Lipid Bilayer ◽  
Metal Ion ◽  
Bilayer Membrane ◽  
Ester Hydrolysis ◽  
Lipid Bilayer Membrane ◽  
Metal Ion Cofactors

Synthetic transducers transport externally added metal ion cofactors across the lipid bilayer membrane of vesicles to trigger catalysis of ester hydrolysis in the inner compartment. Signal transduction activity is modulated by hydrazone formation.

scholarly journals Protein Sensing Device with Multi-Recognition Ability Composed of Self-Organized Glycopeptide Bundle

2020 ◽  
Vol 22 (1) ◽  
pp. 366
Author(s):  
Mao Arai ◽  
Tomohiro Miura ◽  
Yuriko Ito ◽  
Takatoshi Kinoshita ◽  
Masahiro Higuchi
Keyword(s):  
Binding Site ◽  
Lipid Bilayer ◽  
Structural Changes ◽  
Bilayer Membrane ◽  
Lipid Bilayer Membrane ◽  
Target Protein ◽  
Self Organization ◽  
Specific Response ◽  
Target Proteins ◽  
Recognition Ability

We designed and synthesized amphiphilic glycopeptides with glucose or galactose at the C-terminals. We observed the protein-induced structural changes of the amphiphilic glycopeptide assembly in the lipid bilayer membrane using transmission electron microscopy (TEM) and Fourier transform infrared reflection-absorption spectra (FTIR-RAS) measurements. The glycopeptides re-arranged to form a bundle that acted as an ion channel due to the interaction among the target protein and the terminal sugar groups of the glycopeptides. The bundle in the lipid bilayer membrane was fixed on a gold-deposited quartz crystal microbalance (QCM) electrode by the membrane fusion method. The protein-induced re-arrangement of the terminal sugar groups formed a binding site that acted as a receptor, and the re-binding of the target protein to the binding site induced the closing of the channel. We monitored the detection of target proteins by the changes of the electrochemical properties of the membrane. The response current of the membrane induced by the target protein recognition was expressed by an equivalent circuit consisting of resistors and capacitors when a triangular voltage was applied. We used peanut lectin (PNA) and concanavalin A (ConA) as target proteins. The sensing membrane induced by PNA shows the specific response to PNA, and the ConA-induced membrane responded selectively to ConA. Furthermore, PNA-induced sensing membranes showed relatively low recognition ability for lectin from Ricinus Agglutinin (RCA120) and mushroom lectin (ABA), which have galactose binding sites. The protein-induced self-organization formed the spatial arrangement of the sugar chains specific to the binding site of the target protein. These findings demonstrate the possibility of fabricating a sensing device with multi-recognition ability that can recognize proteins even if the structure is unknown, by the protein-induced self-organization process.

Voltage-induced gating of the mechanosensitive MscL ion channel reconstituted in a tethered lipid bilayer membrane

2008 ◽  
Vol 23 (6) ◽  
pp. 919-923 ◽  
Author(s):  
Martin Andersson ◽  
George Okeyo ◽  
Danyell Wilson ◽  
Henk Keizer ◽  
Paul Moe ◽  
...  
Keyword(s):  
Ion Channel ◽  
Lipid Bilayer ◽  
Bilayer Membrane ◽  
Lipid Bilayer Membrane

scholarly journals Fatty Acid Fueled Transmembrane Chloride Transport

2019 ◽  
Author(s):  
Ethan N.W. Howe ◽  
Philip Gale
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Lipid Bilayer ◽  
Chloride Transport ◽  
Bilayer Membrane ◽  
Lipid Bilayer Membrane ◽  
Ph Gradient ◽  
Pumping System ◽  
Membrane Addition

We report an example of the use of fatty acids to drive chloride transport by creating a pH gradient across a vesicular lipid bilayer membrane. Addition of an unselective squaramide-based chloride transporter (which transports both H<sup>+</sup>and Cl<sup>-</sup>) facilitates the transport of HCl from the vesicle (driven by the pH gradient) so creating a chloride gradient. Addition of further aliquots of fatty acid ‘fuel’ can initiate further transport of chloride out of the vesicle by re-establishing the pH gradient. This is an example of a prototypical chloride pumping system.

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