Self-assembly of small-molecule fumaramides allows transmembrane chloride channel formation

2018 ◽  
Vol 54 (16) ◽  
pp. 2024-2027 ◽  
Author(s):  
Arundhati Roy ◽  
Amitosh Gautam ◽  
Javid Ahmad Malla ◽  
Sohini Sarkar ◽  
Arnab Mukherjee ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Ion Channels ◽  
Lipid Bilayer ◽  
Small Molecule ◽  
Chloride Channel ◽  
Self Assembly ◽  
Bilayer Membrane ◽  
Lipid Bilayer Membrane ◽  
Intermolecular Hydrogen Bonding ◽  
Channel Formation

Intermolecular hydrogen bonding of N1,N4-dicyclohexylfumaramide favors the formation of self-assembled ion channels, which facilitates selective Cl− transport across a lipid bilayer 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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