The inhibition effect of amiloride on alamethicin ion channels was studied in a model zwitterionic floating bilayer lipid membrane (fBLM). The EIS studies indicated that amiloride prevents the transport of ions through the alamethicin channels leading to an overall increase in membrane resistance. The PM-IRRAS data demonstrated that amiloride has no influence on the secondary structure of alamethicin but restricts the insertion of the peptides into the bilayer and blocks ion transport through preformed alamethicin channels. The effect of amiloride on ion channel formation in the floating bilayer formed by a zwitterionic lipid was compared to those of previous studies involving negatively charged fBLMs and tethered zwitterionic lipid bilayers. The findings from these studies show that the effects of amiloride on ion channel formation strongly depend on the mobility and charge of the membrane lipids.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/acs.langmuir.2c00953 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Effect of Lipid Composition on the Inhibition Mechanism of Amiloride on Alamethicin Ion Channels in Supported Phospholipid Bilayers.
Langmuir
July 2022
Department of Chemistry, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
The inhibition effect of amiloride on alamethicin ion channels was studied in a model zwitterionic floating bilayer lipid membrane (fBLM). The EIS studies indicated that amiloride prevents the transport of ions through the alamethicin channels leading to an overall increase in membrane resistance. The PM-IRRAS data demonstrated that amiloride has no influence on the secondary structure of alamethicin but restricts the insertion of the peptides into the bilayer and blocks ion transport through preformed alamethicin channels.
View Article and Find Full Text PDFWater Structure in the Submembrane Region of a Floating Lipid Bilayer: The Effect of an Ion Channel Formation and the Channel Blocker.
Langmuir
January 2020
Department of Chemistry , University of Guelph, Guelph , Ontario N1G 2W1 , Canada.
The structure of water in the submembrane region of the bilayer of DPhPC floating (fBLM) on a monolayer of 1-thio-β-d-glucose (β-Tg)-modified gold nanoparticle film was studied by the surface-enhanced infrared absorption spectroscopy (SEIRAS). SEIRAS employs surface enhancement of the mean square electric field of the photon, which is acting on a few molecular layers above the film of gold nanoparticles. Therefore, it is uniquely suited to probe water molecules in the submembrane region and provides unique information concerning the structure of the hydrogen bond network of water surrounding the lipid bilayer.
View Article and Find Full Text PDFEffects of Amiloride, an Ion Channel Blocker, on Alamethicin Pore Formation in Negatively Charged, Gold-Supported, Phospholipid Bilayers: A Molecular View.
Langmuir
April 2019
Department of Chemistry , University of Guelph, Guelph , Ontario , Canada N1G 2W1.
The effects of amiloride on the structure and conductivity of alamethicin ion pore formation within negatively charged, gold-supported, 1,2-dimyristoyl- sn-glycero-3-phosphocholine/Egg-PG membranes were investigated with the help of electrochemical impedance spectroscopy (EIS), photon polarization modulation-infrared reflection spectroscopy (PM-IRRAS), and atomic force microscopy (AFM). The EIS results indicate that ion conductivity across negatively charged phospholipid bilayers containing alamethicin decreases by an order of magnitude when amiloride is introduced to the system. Despite the reduction in ion conductivity, the PM-IRRAS data shows that amiloride does not inhibit ion channel formation by alamethicin peptides.
View Article and Find Full Text PDFA tethered bilayer sensor containing alamethicin channels and its detection of amiloride based inhibitors.
Biosens Bioelectron
April 2003
Australian Membrane Biotechnology Research Institute, 126 Greville Street, Chatswood NSW 2067, Australia.
Alamethicin, a small transmembrane peptide, inserts into a tethered bilayer membrane (tBLM) to form ion channels, which we have investigated using electrical impedance spectroscopy. The number of channels formed is dependent on the incubation time, concentration of the alamethicin and the application of DC voltage. The properties of the ion channels when formed in tethered bilayers are similar to those for such channels assembled into black lipid membranes (BLMs).
View Article and Find Full Text PDFPurified canine cardiac sarcolemmal membrane vesicles exhibit a sodium ion for proton exchange activity (Na+/H+ exchange). Na+/H+ exchange was demonstrated both by measuring rapid 22Na uptake into sarcolemmal vesicles in response to a transmembrane H+ gradient and by following H+ transport in response to a transmembrane Na+ gradient with use of the probe acridine orange. Maximal 22Na uptake into the sarcolemmal vesicles (with starting intravesicular pH = 6 and extravesicular pH = 8) was approximately 20 nmol/mg protein.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!