Water channel formation and ion transport in linear and branched lipid bilayers

2014 ◽  
Vol 16 (16) ◽  
pp. 7251-7262 ◽  
Author(s):  
Shihu Wang ◽  
Ronald G. Larson
Keyword(s):  
Ion Transport ◽  
Lipid Bilayer ◽  
Lipid Bilayers ◽  
Water Channel ◽  
Channel Formation ◽  
Bilayer Stability

The lipid bilayer stability and water channel morphologies are affected by the presence of methyl branches on lipid tails.

Membrane Alterations Induced by Amphiphiles

1989 ◽  
Vol 16 (3) ◽  
pp. 274-280
Author(s):  
Boris Isomaa ◽  
Henry Hägerstrand ◽  
Gun I.L. Paatero
Keyword(s):  
Ion Transport ◽  
Lipid Bilayer ◽  
Erythrocyte Membrane ◽  
Cell Shape ◽  
Osmotic Fragility ◽  
Molecular Shape ◽  
Specific Interactions ◽  
Amphiphilic Compounds ◽  
Rapid Formation ◽  
Polar Parts

Amphiphilic compounds with distinct apolar and polar parts are readily intercalated into the erythrocyte membrane. When intercalated into the membrane, amphiphiles are probably orientated so that the polar head is at the polar-apolar interface of the lipid bilayer and the hydrophobic part within the apolar core of the bilayer. However, by virtue of their difference in molecular shape from the bulk lipids of the lipid bilayer, it is possible that the intercalated amphiphiles are partly segregated from bulk lipids and accumulate at protein-lipid interfaces in the bilayer, where the packing of the bilayer lipids may be less ordered. Our studies show that amphiphiles, when intercalated into the erythrocyte membrane, trigger alterations in several membrane-connected functions. Some of the alterations induced (decreased osmotic fragility, increased passive potassium fluxes) seem to be due to non-specific interactions of the amphiphiles with the membrane, whereas other functions (ion transport mediated by membrane proteins, regulation of cell shape) seem to be sensitive to particular features of the amphiphiles. Our studies indicate that the intercalation of amphiphiles into the erythrocyte membrane must involve rearrangements within the lipid bilayer. We have suggested that, when intercalated into the lipid bilayer, amphiphiles trigger a rapid formation of non-bilayer phases, which protect the bilayer against a collapse and bring about a trans-bilayer redistribution of intercalated amphiphiles as well as of bilayer lipids. At high sublytic concentrations, this process may also involve a release of microvesicles from the membrane.

scholarly journals Tentative Peptide‒Lipid Bilayer Models Elucidating Molecular Behaviors and Interactions Driving Passive Cellular Uptake of Collagen-Derived Small Peptides

Molecules ◽  
2021 ◽  
Vol 26 (3) ◽  
pp. 710
Author(s):  
Pathomwat Wongrattanakamon ◽  
Wipawadee Yooin ◽  
Busaban Sirithunyalug ◽  
Piyarat Nimmanpipug ◽  
Supat Jiranusornkul
Keyword(s):  
Lipid Bilayer ◽  
Lipid Bilayers ◽  
Mean Square Displacement ◽  
Dynamics Simulation ◽  
Coordinate Frame ◽  
Mean Square ◽  
Binding Modes ◽  
Small Peptides ◽  
Collagen Peptides ◽  
Electron Density Profiles

Collagen contains hydroxyproline (Hyp), which is a unique amino acid. Three collagen-derived small peptides (Gly-Pro-Hyp, Pro-Hyp, and Gly-Hyp) interacting across a lipid bilayer (POPC model membrane) for cellular uptakes of these collagen-derived small peptides were studied using accelerated molecular dynamics simulation. The ligands were investigated for their binding modes, hydrogen bonds in each coordinate frame, and mean square displacement (MSD) in the Z direction. The lipid bilayers were evaluated for mass and electron density profiles of the lipid molecules, surface area of the head groups, and root mean square deviation (RMSD). The simulation results show that hydrogen bonding between the small collagen peptides and plasma membrane plays a significant role in their internalization. The translocation of the small collagen peptides across the cell membranes was shown. Pro-Hyp laterally condensed the membrane, resulting in an increase in the bilayer thickness and rigidity. Perception regarding molecular behaviors of collagen-derived peptides within the cell membrane, including their interactions, provides the novel design of specific bioactive collagen peptides for their applications.

Potassium Ion Transport by Valinomycin across a Hg-Supported Lipid Bilayer

2005 ◽  
Vol 127 (38) ◽  
pp. 13316-13323 ◽  
Author(s):  
Lucia Becucci ◽  
Maria Rosa Moncelli ◽  
Renate Naumann ◽  
Rolando Guidelli
Keyword(s):  
Ion Transport ◽  
Lipid Bilayer ◽  
Potassium Ion ◽  
Supported Lipid Bilayer ◽  
Potassium Ion Transport

scholarly journals Lipid bilayer degradation induced by SARS-CoV-2 spike protein as revealed by neutron reflectometry

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Alessandra Luchini ◽  
Samantha Micciulla ◽  
Giacomo Corucci ◽  
Krishna Chaithanya Batchu ◽  
Andreas Santamaria ◽  
...  
Keyword(s):  
Lipid Bilayer ◽  
Lipid Bilayers ◽  
Membrane Lipids ◽  
Lipid Extraction ◽  
Specific Interaction ◽  
Structural Features ◽  
Supported Lipid Bilayers ◽  
Fusion Event ◽  
Angiotensin Converting Enzyme 2 ◽  
Neutron Reflection

AbstractSARS-CoV-2 spike proteins are responsible for the membrane fusion event, which allows the virus to enter the host cell and cause infection. This process starts with the binding of the spike extramembrane domain to the angiotensin-converting enzyme 2 (ACE2), a membrane receptor highly abundant in the lungs. In this study, the extramembrane domain of SARS-CoV-2 Spike (sSpike) was injected on model membranes formed by supported lipid bilayers in presence and absence of the soluble part of receptor ACE2 (sACE2), and the structural features were studied at sub-nanometer level by neutron reflection. In all cases the presence of the protein produced a remarkable degradation of the lipid bilayer. Indeed, both for membranes from synthetic and natural lipids, a significant reduction of the surface coverage was observed. Quartz crystal microbalance measurements showed that lipid extraction starts immediately after sSpike protein injection. All measurements indicate that the presence of proteins induces the removal of membrane lipids, both in the presence and in the absence of ACE2, suggesting that sSpike molecules strongly associate with lipids, and strip them away from the bilayer, via a non-specific interaction. A cooperative effect of sACE2 and sSpike on lipid extraction was also observed.

Effect of Sterol Side Chain on Ion Channel Formation by Amphotericin B in Lipid Bilayers

Biochemistry ◽  
2014 ◽  
Vol 53 (19) ◽  
pp. 3088-3094 ◽  
Author(s):  
Yasuo Nakagawa ◽  
Yuichi Umegawa ◽  
Tetsuro Takano ◽  
Hiroshi Tsuchikawa ◽  
Nobuaki Matsumori ◽  
...  
Keyword(s):  
Ion Channel ◽  
Amphotericin B ◽  
Lipid Bilayers ◽  
Side Chain ◽  
Channel Formation

scholarly journals Surface roughness as rupture control factor of lipid vesicles

2013 ◽  
Vol 19 (S4) ◽  
pp. 107-108 ◽  
Author(s):  
A.A. Duarte ◽  
M. Raposo
Keyword(s):  
Lipid Bilayer ◽  
Lipid Bilayers ◽  
Biological Membrane ◽  
Substrate Surface ◽  
Lipid Vesicles ◽  
Planar Lipid Bilayer ◽  
Root Mean Square Roughness ◽  
Control Factor ◽  
Formation Mechanisms ◽  
Adsorbed Amount

Liposomes or lipid vesicles are self-closed structures formed by one or several concentric lipid bilayers with an aqueous phase inside, which may incorporate almost any molecule, namely proteins, hormones, enzymes, antibiotics, anticancer agents, antifungical agents, gene transfer agents, DNA, and whole viruses. Scientific evidences prove that unprotected liposomes containing drugs are easily released from the endoplasmic reticulum of the cell. To increase the vesicles lifetime and to activate a controlled drug release with an external stimulus, the vesicles immobilization on a surface and the factors which create conditions to the liposome rupture have to be analyzed. A number of studies have identified some of the critical stages of vesicle adsorption (adhesion), fusion, deformation, rupture, and spreading of the lipid bilayer. Nevertheless, the formation mechanisms of well-controlled continuous supported bilayers or adsorption of whole liposomes are still not fully understood. As yet it was demonstrated that a controlled adsorption of vesicles containing a small fraction of charged lipids occurs without rupture and their subsequent embedding in polyelectrolyte multilayer (PEM) films, meaning vesicles may be immobilized in an intact or slightly deformed state, which can act as drug reservoirs. Moreover, depending on the nature of the physicochemical conditions of the vesicle solution and the substrate surface, a flat lipid bilayer can be formed, known as supported lipid bilayers, which can incorporate membrane proteins and keep the native dynamics of the lipid bilayer mimicking a biological membrane. In this study, a layer of 1,2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt) (DPPG) liposomes adsorbed onto PEMs cushions based on poly(ethylenimine) (PEI), poly(sodium 4-styrenesulfonate) (PSS) and poly(allylamine hydrochloride) (PAH) polyelectrolytes was analyzed by atomic force microscopy (AFM) technique in non-contact mode and quartz crystal microbalance (QCM).Sequential heterostructures of Si/PEI(PSS/PAH)4 and Si/PAH, also designated cushions, were prepared onto silicon substrates using the layer-by-layer (LbL) technique with polyelectrolyte solutions of PEI, PSS and PAH of monomeric concentrations of 0.01M. Topographic images of 1×1μm2 area of Si/PAH/DPPG (Figure 1 a), and Si/PEI(PSS/PAH)4/DPPG (Figure 1 b) LbL films were acquired by AFM. The root mean square roughness (RMS) calculated from topographies data are listed in table I. As shown, when a DPPG layer is adsorbed onto Si/PAH the RMS keeps an approximately equal value meaning that the liposome disrupted and spread onto the surface forming a planar lipid bilayer. But when a DPPG layer is adsorbed onto Si/PEI(PSS/PAH)4 the RMS value doubled, indicating that the structural integrity of the liposomes is maintained, even though there has been any deformation during adsorption. The adsorbed amount of the two PEMs and DPPG-liposomes layers was measured using a QCM and is displayed in table I. The DPPG adsorbed amount obtained on the PAH cushion was approximately equal to a planar lipid bilayer, while the adsorption onto PEI(PSS/PAH)4 was higher than the predicted for a planar lipid bilayer. This behavior suggests that the DPPG liposomes on the second PEM remained intact during adsorption. Both confirm the AFM results. Therefore we conclude that the initial roughness of the surface is a primordial factor to determine the adsorption or not of intact vesicles.The authors acknowledge the “Fundação para a Ciência e Tecnologia” (FCT-MEC) by the post-graduate scholarship SFRH/BD/62229/2009 and the “Plurianual” funding.

scholarly journals Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein

2021 ◽  
Vol 119 (1) ◽  
pp. e2109169119
Author(s):  
Kristen A. Gaffney ◽  
Ruiqiong Guo ◽  
Michael D. Bridges ◽  
Shaima Muhammednazaar ◽  
Daoyang Chen ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Lipid Bilayer ◽  
Lipid Bilayers ◽  
Limited Proteolysis ◽  
Water Soluble ◽  
Disordered Proteins ◽  
Resonance Spectroscopy ◽  
Denatured State ◽  
E Coli ◽  
State Ensemble

Defining the denatured state ensemble (DSE) and disordered proteins is essential to understanding folding, chaperone action, degradation, and translocation. As compared with water-soluble proteins, the DSE of membrane proteins is much less characterized. Here, we measure the DSE of the helical membrane protein GlpG of Escherichia coli (E. coli) in native-like lipid bilayers. The DSE was obtained using our steric trapping method, which couples denaturation of doubly biotinylated GlpG to binding of two streptavidin molecules. The helices and loops are probed using limited proteolysis and mass spectrometry, while the dimensions are determined using our paramagnetic biotin derivative and double electron–electron resonance spectroscopy. These data, along with our Upside simulations, identify the DSE as being highly dynamic, involving the topology changes and unfolding of some of the transmembrane (TM) helices. The DSE is expanded relative to the native state but only to 15 to 75% of the fully expanded condition. The degree of expansion depends on the local protein packing and the lipid composition. E. coli’s lipid bilayer promotes the association of TM helices in the DSE and, probably in general, facilitates interhelical interactions. This tendency may be the outcome of a general lipophobic effect of proteins within the cell membranes.

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