scholarly journals Ionophore-mediated transmembrane movement of divalent cations in small unilamellar liposomes: An evaluation of the chlortetracycline fluorescence technique and correlations with black lipid membrane studies

1982 ◽  
Vol 65 (1-2) ◽  
pp. 13-17 ◽  
Author(s):  
M. K. Mathew ◽  
R. Nagaraj ◽  
P. Balaram
Keyword(s):  
Lipid Membrane ◽  
Divalent Cations ◽  
Fluorescence Technique ◽  
Black Lipid Membrane

scholarly journals The Main (Glyco) Phospholipid (MPL) of Thermoplasma acidophilum

2019 ◽  
Vol 20 (20) ◽  
pp. 5217
Author(s):  
Hans-Joachim Freisleben
Keyword(s):  
Lipid Membrane ◽  
Micrococcus Luteus ◽  
Atp Synthesis ◽  
Scanning Calorimetry ◽  
Thermoplasma Acidophilum ◽  
Black Lipid Membrane ◽  
Langmuir Blodgett ◽  
Hydrophobic Peptides ◽  
Laboratory Results ◽  
Review Reports

The main phospholipid (MPL) of Thermoplasma acidophilum DSM 1728 was isolated, purified and physico-chemically characterized by differential scanning calorimetry (DSC)/differential thermal analysis (DTA) for its thermotropic behavior, alone and in mixtures with other lipids, cholesterol, hydrophobic peptides and pore-forming ionophores. Model membranes from MPL were investigated; black lipid membrane, Langmuir-Blodgett monolayer, and liposomes. Laboratory results were compared to computer simulation. MPL forms stable and resistant liposomes with highly proton-impermeable membrane and mixes at certain degree with common bilayer-forming lipids. Monomeric bacteriorhodopsin and ATP synthase from Micrococcus luteus were co-reconstituted and light-driven ATP synthesis measured. This review reports about almost four decades of research on Thermoplasma membrane and its MPL as well as transfer of this research to Thermoplasma species recently isolated from Indonesian volcanoes.

scholarly journals Lipid II-Mediated Pore Formation by the Peptide Antibiotic Nisin: a Black Lipid Membrane Study

2004 ◽  
Vol 186 (10) ◽  
pp. 3259-3261 ◽  
Author(s):  
Imke Wiedemann ◽  
Roland Benz ◽  
Hans-Georg Sahl
Keyword(s):  
Cell Wall ◽  
Pore Formation ◽  
Cytoplasmic Membrane ◽  
Lipid Membrane ◽  
Specific Interaction ◽  
Peptide Antibiotic ◽  
Black Lipid Membrane ◽  
Lipid Ii ◽  
Antibiotic Peptide

ABSTRACT The antibiotic peptide nisin is the first known lantibiotic that uses a docking molecule within the bacterial cytoplasmic membrane for pore formation. Through specific interaction with the cell wall precursor lipid II, nisin forms defined pores which are stable for seconds and have pore diameters of 2 to 2.5 nm.

Improved Parameterization of Phosphatidylinositide Lipid Headgroups for the Martini 3 Coarse Grain Force Field

2021 ◽  
Author(s):  
Luis Borges-Araújo ◽  
Paulo Souza ◽  
Fábio Fernandes ◽  
Manuel N. Melo
Keyword(s):  
Force Field ◽  
Lipid Membrane ◽  
Divalent Cations ◽  
Conformational Dynamics ◽  
Experimental Studies ◽  
Dynamics Simulation ◽  
Coarse Grain ◽  
Membrane Phospholipids ◽  
Martini Force Field ◽  
Derivatives Of

Phosphoinositides are a family of membrane phospholipids that play crucial roles in membrane regulatory events. As such, these lipids are often a key part of molecular dynamics simulation studies of biological membranes, in particular of those employing coarse-grain models because of the potential long times and sizes of the involved membrane processes. Version 3 of the widely used Martini coarse grain force field has been recently published, greatly refining many aspects of biomolecular interactions. In order to properly use it for lipid membrane simulations with phosphoinositides, we put forth the Martini 3-specific parameterization of inositol, phosphatidylinositol, the seven physiologically relevant phosphorylated derivatives of phosphatidylinositol. Compared to parameterizations for earlier Martini versions, focus was put on a more accurate reproduction of the behavior seen in both atomistic simulations and experimental studies, including the signaling relevant phosphoinositide interaction with divalent cations. The models we develop improve upon the conformational dynamics of phosphoinositides in the Martini force field and provide stable topologies at typical Martini timesteps. They are able to reproduce experimentally known protein-binding poses as well as phosphoinositide aggregation tendencies. The latter were tested both in the presence and absence of calcium, and include correct behavior of PI(4,5)P2 calcium-induced clusters, which can be of relevance for regulation.

Electronic Conduction across a Black Lipid Membrane

Nature ◽  
1970 ◽  
Vol 227 (5259) ◽  
pp. 705-707 ◽  
Author(s):  
MAHENDRA K. JAIN ◽  
ALFRED STRICKHOLM ◽  
FREDERICK P. WHITE ◽  
E. H. CORDES
Keyword(s):  
Lipid Membrane ◽  
Electronic Conduction ◽  
Black Lipid Membrane

scholarly journals Improved Parameterization of Phosphatidylinositide Lipid Headgroups for the Martini 3 Coarse Grain Force Field

2021 ◽  
Author(s):  
Luis Borges-Araújo ◽  
Paulo Souza ◽  
Fábio Fernandes ◽  
Manuel N. Melo
Keyword(s):  
Force Field ◽  
Lipid Membrane ◽  
Divalent Cations ◽  
Conformational Dynamics ◽  
Experimental Studies ◽  
Dynamics Simulation ◽  
Coarse Grain ◽  
Membrane Phospholipids ◽  
Martini Force Field ◽  
Derivatives Of

Phosphoinositides are a family of membrane phospholipids that play crucial roles in membrane regulatory events. As such, these lipids are often a key part of molecular dynamics simulation studies of biological membranes, in particular of those employing coarse-grain models because of the potential long times and sizes of the involved membrane processes. Version 3 of the widely used Martini coarse grain force field has been recently published, greatly refining many aspects of biomolecular interactions. In order to properly use it for lipid membrane simulations with phosphoinositides, we put forth the Martini 3-specific parameterization of inositol, phosphatidylinositol, the seven physiologically relevant phosphorylated derivatives of phosphatidylinositol. Compared to parameterizations for earlier Martini versions, focus was put on a more accurate reproduction of the behavior seen in both atomistic simulations and experimental studies, including the signaling relevant phosphoinositide interaction with divalent cations. The models we develop improve upon the conformational dynamics of phosphoinositides in the Martini force field and provide stable topologies at typical Martini timesteps. They are able to reproduce experimentally known protein-binding poses as well as phosphoinositide aggregation tendencies. The latter were tested both in the presence and absence of calcium, and include correct behavior of PI(4,5)P2 calcium-induced clusters, which can be of relevance for regulation.

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