Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Lipid Bilayers”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1984

Interaction of influenza virus proteins with planar bilayer lipid membranes. I. Characterization of their adsorption and incorporation into lipid bilayers.

Alterations in the surface potential difference (delta U) of asolectin planar bilayer lipid membranes were measured following the adsorption of isolated matrix protein (M-protein) or neuraminidase of influenza virus. The method used was based upon measurement of the bilayer lipid membrane capacitance current second harmonic. The delta U dependence on the M-protein and neuraminidase concentration indicates different mechanisms of adsorption of these viral proteins by the lipid bilayer. The conductance (G0) dependence of the bilayer lipid membrane with different compositions on the concentration of isolated surface glycoproteins, hemagglutinin and neuraminidase, M-protein or neuraminidase was investigated. The change in G0 for M-protein was observed only after adsorption saturation had been achieved. Neuraminidase alone does not affect the membrane conductivity. The surface charge and lipid composition of the lipid bilayer influences the adsorption and incorporation of influenza virus M-protein and surface glycoproteins. The reversibility of protein incorporation into the bilayers was investigated by a perfusion technique. The results show reversibility of surface glycoprotein incorporation while M-protein binding appears to be irreversible.

Adsorption↗
PubMed2005

Gravimetric antigen detection utilizing antibody-modified lipid bilayers.

Lipid bilayers containing 5% nitrilotriacetic acid (NTA) lipids supported on SiO2 have been used as a template for immobilization of oligohistidine-tagged single-chained antibody fragments (scFvs) directed against cholera toxin. It was demonstrated that histidine-tagged scFvs could be equally efficiently coupled to an NTA-Ni2+-containing lipid bilayer from a purified sample as from an expression supernatant, thereby providing a coupling method that eliminates time-consuming protein prepurification steps. Irrespective of whether the coupling was made from the unpurified or purified antibody preparation, the template proved to be efficient for antigen (cholera toxin) detection, verified using quartz crystal microbalance with dissipation monitoring. In addition, via a secondary amplification step using lipid vesicles containing GM1 (the natural membrane receptor for cholera toxin), the detection limit of cholera toxin was less than 750 pM. To further strengthen the coupling of scFvs to the lipid bilayer, scFvs containing two histidine tags, instead of just one tag, were also evaluated. The increased coupling strength provided via the bivalent anchoring significantly reduced scFv displacement in complex solutions containing large amounts of histidine-containing proteins, verified via cholera toxin detection in serum.

Biological Assay↗
PubMed1995

The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer.

Lipids and proteins were found to contact a nascent type II membrane protein, as well as a nascent secretory protein, during their insertion into the membrane of the endoplasmic reticulum. This suggests that the protein-conducting channel is open laterally toward the lipid bilayer during an early stage of protein insertion. Contact to lipids was confined to the hydrophobic core region of the respective signal or signal anchor sequence. Thus, the nascent polypeptide is positioned in the translocation complex such that the signal or signal anchor sequence faces the lipid bilayer, whereas the hydrophilic, translocating portion is in proteinaceous environment.

Antigens, Differentiation, B-Lymphocyte↗
PubMed1984

Formation and properties of tetramers of band 3 protein from human erythrocyte membranes in planar lipid bilayers.

Lipid bilayer experiments were performed in the presence of solubilized band 3 protein from human red cell membranes. Band 3 protein increased the conductance of the lipid membranes by several orders of magnitude. Membrane conductance was found to be dependent on the fourth power of protein concentration. This shows that four band 3 subunits form an ion permeable pathway in the lipid bilayer membranes. It also shows that, in the membranes, the protein molecules undergo an association equilibrium which involves at least the monomer and the tetramer of the protein, relaxation towards equilibrium being rapid on the time scale of the experiment. The increase in bilayer conductance induced by the band 3 tetramer could be inhibited by pretreatment of the protein with several SH-reagents (pCMB, pCMBS, DTNB) which also inhibit water transport across the human red cell membrane. Other SH-reagents which do not influence water transport (iodoacetamide, N-ethylmaleimide) did not show any influence on the band 3 induced conductance increase. A band 3-mediated exchange of anions comparable to that in the erythrocyte membrane did not occur in the system studied by us. Our results suggest that, in the human erythrocyte membrane, a pore formed by the band 3 tetramer could be the pathway responsible for the protein-mediated part of water transport.

4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid↗
PubMed2005

Density functional theory approach for coarse-grained lipid bilayers.

Lipid bilayers are important inhomogeneous fluid systems that mediate the environment of cells and the interaction of cells with their environment. A variety of approaches have been taken to model the lipid molecules in bilayers, from all atom molecular dynamics to rigid body liquid crystals. In this paper we discuss the application of a density functional theory approach that treats the lipid molecules at the coarse-grained level of a freely jointed chain. This approach allows for compressibility effects, and can therefore be used to study not only the long range structure in lipid bilayers, but also the nanoscale structure induced in the bilayer when the lipids crystallize or when an inclusion (e.g., an embedded protein) is present. This paper presents a detailed analysis of fluid bilayers and lamellae predicted by the theory. In particular we locate solutions with zero surface tension. We calculate the phase diagram for all possible phases with planar symmetry, including uniform macrophases. Surprisingly, we find a first-order phase transition from the lamellar phase to an isolated bilayer phase on lowering the temperature. This transition appears to be driven by solvent packing effects. A further lowering of the temperature leads to a set of highly ordered bilayers.

Computer Simulation↗
PubMed1996

Non-bilayer lipids and biological fusion intermediates.

Disparate biological fusion reactions and fusion of purely lipid bilayers are similarly influenced by 'non-bilayer' lipids (lipids which do not form lipid bilayers in water by themselves). Lipid composition of membranes affects biological fusion at a stage downstream of activation of fusion proteins and prior to fusion pore formation. These data suggest that actual merger of membrane lipid bilayers in different fusion reactions proceeds via the same pathway. The effects of non-bilayer lipids specifically correlate with their ability to bend lipid monolayers in different directions, and appear to be consistent with the specific hypothesis of membrane fusion suggesting that fusion proceeds through highly bent intermediates--stalks, local connections between contacting monolayers of fusing membranes.

Hydrogen-Ion Concentration↗
PubMed2002

Nonequilibrium phenomena in the phase separation of a two-component lipid bilayer.

Lipid bilayers composed of two phospholipids with significant acyl-chain mismatch behave as nonideal mixtures. Although many of these systems are well characterized from the equilibrium point of view, studies concerning their nonequilibrium dynamics are still rare. The kinetics of lipid demixing (phase separation) was studied in model membranes (large unilamellar vesicles of 1:1 dilauroylphosphatidylcholine (C(12) acyl chain) and distearoylphosphatidylcholine (C(18) acyl chain)). For this purpose, photophysical techniques (fluorescence intensity, anisotropy, and fluorescence resonance energy transfer) were applied using suitable probes (gel phase probe trans-parinaric acid and fluid phase probe N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-dilauroylphosphatidylethanolamine). The nonequilibrium situation was induced by a sudden thermal quench from a one-fluid phase equilibrium situation (higher temperature) to the gel/fluid coexistence range (lower temperature). We verified that the attainment of equilibrium is a very slow process (occurs in a time scale of hours), leading to large domains at infinite time. The nonequilibrium structure stabilization is due essentially to temporarily rigidified C(12) chains in the interface between gel/fluid domains, which decrease the interfacial tension by acting as surfactants. The relaxation process becomes faster with the increase of the temperature drop. In addition, heterogeneity is already present in the supposed homogeneous fluid mixture at the higher temperature.

Anisotropy↗
PubMed2003

Growth of cationic lipid toward bilayer lipid membrane by solution spreading: scanning probe microscopy study.

The growth of cationic lipid dioctadecyldimethylammonium bromide (DODAB) toward bilayer lipid membrane (BLM) by solution spreading on cleaved mica surface was studied by atomic force microscopy (AFM). Bilayer of DODAB was formed by exposing mica to a solution of DODAB in chloroform and subsequently immersing into potassium chloride solution for film developing. AFM studies showed that at the initial stage of the growth, the adsorbed molecules exhibited the small fractal-like aggregates. These aggregates grew up and expanded laterally into larger patches with time and experienced from monolayer to bilayer, finally a close-packed bilayer film (5.4+/-0.2 nm) was approached. AFM results of the film growth process indicated a growth mechanism of nucleation, growth and coalescence of dense submonolayer, it revealed the direct information about the film morphology and confirmed that solution spreading was an effective technique to prepare a cationic bilayer in a short time.

Aluminum Silicates↗
PubMed2004

Tethered bilayer lipid membranes self-assembled on mercury electrodes.

In order to incorporate integral proteins in a functionally active state, metal-supported lipid bilayers must have a hydrophilic region interposed between the bilayer and the metal. This region is realized with a hydrophilic molecule terminating at one end with a sulfhydryl or disulfide group that anchors this "hydrophilic spacer" to the surface of a metal, such as gold or mercury. The other end of the hydrophilic spacer may be covalently linked to the polar head of a phospholipid molecule, giving rise to a supramolecule called "thiolipid" (TL). With respect to gold, mercury has the advantage of providing a defect-free and fluid surface to the self-assembling spacer. Hydrophilic spacers consisting of a polyethyleneoxy or a hexapeptide chain, as well as thiolipids derived from these spacers, were employed to fabricate mercury-supported lipid bilayers. The formation of a lipid bilayer on top of a self-assembled monolayer of a hydrophilic spacer, or of a single-lipid monolayer on top of a self-assembled monolayer of a thiolipid, was realized by simply immersing the coated mercury electrode into an aqueous solution across a lipid film previously spread on its surface at its spreading pressure. Particularly stable mercury-supported lipid bilayers were obtained by using thiolipids. The biomimetic properties of these lipid bilayers were tested by incorporating channel-forming polypeptides (gramicidin and melittin) and proteins (OmpF porin). The effect of the transmembrane potential on the function of these channels was estimated by using a simple electrostatic model of the mercury-solution interphase.

Biomimetic Materials↗
PubMed1994

Lysophospholipids modulate channel function by altering the mechanical properties of lipid bilayers.

Lipid metabolites, free fatty acids and lysophospholipids, modify the function of membrane proteins including ion channels. Such alterations can occur through signal transduction pathways, but may also result from "direct" effects of the metabolite on the protein. To investigate possible mechanisms for such direct effects, we examined the alterations of gramicidin channel function by lysophospholipids (LPLs): lysophosphatidylcholine (LPC), lysophosphatidylethanolamine (LPE), lysophosphatidylserine (LPS), and lysophosphatidylinositol (LPI). The experiments were done on planar bilayers formed by diphytanoylphosphatidylcholine in n-decane a system where receptor-mediated effects can be excluded. At aqueous concentrations below the critical micelle concentration (CMC), LPLs can increase the dimerization constant for membrane-bound gramicidin up to 500-fold (at 2 microM). The relative potency increases as a function of the size of the polar head group, but does not seem to vary as a function of head group charge. The increased dimerization constant results primarily from an increase in the rate constant for channel formation, which can increase more than 100-fold (in the presence of LPC and LPI), whereas the channel dissociation rate constant decreases only about fivefold. The LPL effect cannot be ascribed to an increased membrane fluidity, which would give rise to an increased channel dissociation rate constant. The ability of LPC to decrease the channel dissociation rate constant varies as a function of channel length (which is always less than the membrane's equilibrium thickness): as the channel length is decreased, the potency of LPC is increased. LPC has no effect on membrane thickness or the surface tension of monolayers at the air/electrolyte interface. The bilayer-forming glycerolmonooleate does not decrease the channel dissociation rate constant. These results show that LPLs alter gramicidin channel function by altering the membrane deformation energy, and that the changes in deformation energy can be related to the molecular "shape" of the membrane-modifying compounds. Similar alterations in the mechanical properties of biological membranes may form a general mechanism by which one can alter membrane protein function.

Amino Acid Sequence↗
PubMedDate not supplied

[Formation of stabile cupola-like lipid bilayer membranes with a mobile plateau Gibbs boundary].

Stable bilayer lipid membrane with mobile Platear-Gibbs border have been formed. The predominant condition of the formation is the presence of lipid coverage on the teflon surface near the hole. The formation process includes transformation of the initial planar lipid bilayer into cupola-shaped one by bowing of the lipid bilayer due to hydrostatic pressure, movement of the PGb along the teflon surface. The bilayer area estimated by electric capacitance increases from 0.1 x 10(-8) F to 21 x 10(-8) F. Electric conductance of the lipid bilayer has not changed except for the phase transition and membrane collapse. The electric capacitance of the BLM formed from hydrogenated egg lecithin was changed by cooling between 60 degrees and 40 degrees C with the maximum at about phase transition range. The individual membrane sustains several scannings of the temperature without disruption which is an evidence of the stability of the cupola-shaped membranes.

Electric Conductivity↗
PubMed2004

Soft perforation of planar bilayer lipid membranes of dipalmitoylphosphatidylcholine at the temperature of the phase transition from the liquid crystalline to the gel state.

In contrast to the widely used method of electroporation, the method of soft perforation of lipid bilayers is proposed. It is based on the structural rearrangement of the lipid bilayer formed from disaturated phospholipids at the temperature of the phase transition from the liquid crystalline state to the gel state. This allows us to obtain a lipid pore population without the use of a strong electric field. It is shown that the planar lipid bilayer membrane (pBLM) formed from dipalmitoylphosphatidylcholine in 1 M LiCl aqueous solution exhibits the appearance of up to 50 lipid pores per 1 mm(2) of membrane surface, with an average single pore conductivity of 31 +/- 13 nS. The estimation of a single pore radius carried out with water-soluble poly(ethylene glycol)s (PEGs) showed that the average pore radius ranged between 1.0-1.7 nm. It was found experimentally that PEG-1450, PEG-2000, and PEG-3350 should be in a position to block the single pore conductivity completely, while PEG-6000 fully restored the ionic conductivity. The similarity of these PEG effects to ionic conductivity in protein pores makes it possible to suggest that the partition of the PEG molecules between the pore and the bulk solution does not depend on the nature of the chemical groups located in the pore wall.

Crystallization↗
PubMedDate not supplied

[Elastic properties of lipid bilayer membranes during incorporation of plasma lipoproteins].

Interaction between lipoproteins of very low density /LPVLD/ with bilayer lipid membranes was studied in blood plasma of healthy rabbits and in rabbits with alimentary hyperlipoproteinemia. The LPVLD of healthy animals did not produce any alterations in elasticity and volume of bilayer lipid membranes within 120 sec, whereas the lipid fraction from animals with hyperlipoproteinemia altered these physical properties of the membranes at the period studied. The factors, which are responsible for the action of LPVLD on the bilayer lipid membranes, were both composition and structure of lipoprotein particles. The importance of nitial parameters of the membrane structure in its interaction with lipoproteins was shown using the model system.

Animals↗
PubMed2006

Actin and amphiphilic polymers influence on channel formation by Syringomycin E in lipid bilayers.

The bacterial lipodepsipeptide syringomycin E (SRE) added to one (cis-) side of bilayer lipid membrane forms voltage dependent ion channels. It was found that G-actin increased the SRE-induced membrane conductance due to formation of additional SRE-channels only in the case when actin and SRE were applied to opposite sides of a lipid bilayer. The time course of conductance relaxation depended on the sequence of SRE and actin addition, suggesting that actin binds to the lipid bilayer and binding is a limiting step for SRE-channel formation. G-actin adsorption on the membrane was irreversible. The amphiphilic polymers, Konig's polyanion (KP) and poly(Lys, Trp) (PLT) produced the actin-like effect. It was shown that the increase in the SRE membrane activity was due to hydrophobic interactions between the adsorbing molecules and membrane. Nevertheless, hydrophobic interactions were not sufficient for the increase of SRE channel-forming activity. The dependence of the number of SRE-channels on the concentration of adsorbing species gave an S-shaped curve indicating cooperative adsorption of the species. Kinetic analysis of SRE-channel number growth led to the conclusion that the actin, KP, and PLT molecules form aggregates (domains) on the trans-monolayer. It is suggested that an excess of SRE-channel formation occurs within the regions of the cis-monolayer adjacent to the domains of the adsorbed molecules, which increase the effective concentration of SRE-channel precursors.

Actins↗
PubMed2002

Inter-pulse interval between rectangular voltage pulses affects electroporation threshold of artificial lipid bilayers.

This paper describes experiments that determine how the inter-pulse interval between rectangular pulses in a train of pulses alters the threshold of electroporation of 1-pamitoyl 2-oleoyl phosphatidycholine bilayer lipid membranes. The bilayers were exposed to a train of sixteen 100-micros duration pulses. Threshold voltage and the sequence number of the pulse in the train, where onset of the electroporation occurred, were recorded for six inter-pulse intervals (infinity, 1000 micros, 100 micros, 10 micros, 1 micros, 0 micros). The threshold voltage of the pulse train decreased linearly with the logarithm of the inter-pulse interval. When the inter-pulse interval was 1 microm, electroporation threshold dropped to that of a single pulse with duration 1600 micros (equal to the sum of all pulse durations in the train). In this case, the occurrence of bilayer rupture was almost equally frequent for all pulses in the train. When the inter-pulse interval between the pulses exceeded 1 micros, the influence of the previous pulse on the response to the following pulse declined. It became more likely that the bilayer ruptured during the first half of the train. These experimental observations suggest that a train of pulses applied with short inter-pulse interval (less than 1 ms) can lower the electroporation threshold of bilayer lipid membranes.

Dose-Response Relationship, Drug↗
PubMedDate not supplied

[A soft poration of planar bilayer lipid membranes from dipalmitoylphosphatidylcholine at the temperature of the phase transition from the liquid crystalline to the gel state].

A method of soft poration of lipid bilayer was suggested, which is based on the structural rearrangement of lipid bilayer formed from disaturated phospholipids on the phase transition from liquid crystalline state to the gel. As opposed to the widely used method of electropbration, this method allows one to obtain a lipid pore population without application of high electric field. In the case of soft poration, the electric field does not exceed the physiological level of 10-100 mV. It was shown that, in planar bilayer lipid membranes formed from dipalmitoylphosphatidylcholine in water solution of 1 M LiCl, there appear up to 10 lipid pores in 1 min per 1 mm of membrane surface with an average conductivity of a pore of 31 +/- 13 nS. The average pore radius estimated using soluble polyethylene glycols ranged between 1.05-1.63 nm. Monovalent cation conductivity of a single lipid pore on soft poration was shown to decrease in the order Li+ > or = Na+ > K+ = Rb+ > or = Cs+. This order coincides with that observed by Marra and Israilashvili for dipalmitoylphosphatidylcholine-water interbilayer where the repulsive hydration force contribution is significant.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed2000

Mixed micelles and other structures in the solubilization of bilayer lipid membranes by surfactants.

The solubilization of lipid bilayers by surfactants is accompanied by morphological changes of the bilayer and the emergence of mixed micelles. From a phase equilibrium perspective, the lipid/surfactant/water system is in a two-phase area during the solubilization: a phase containing mixed micelles is in equilibrium with bilayer structures of the lamellar phase. In some cases three phases are present, the single micelle phase replaced by a concentrated and a dilute solution phase. In the case of non-ionic surfactants, the lipid bilayers reach saturation when mixed micelles, often flexible rod-like or thread-like, start to form in the aqueous solution, at a constant chemical potential of the surfactant. The composition of the bilayers also remains fixed during the dissolution. The phase behavior encountered with many charged surfactants is different. The lamellar phase becomes destabilized at a certain content of surfactant in the membrane, and then disintegrates, forming mixed micelles, or a hexagonal phase, or an intermediate phase. Defective bilayer intermediates, such as perforated vesicles, have been found in several systems, mainly with charged surfactants. The perforated membranes, in some systems, go over into thread-like micelles via lace-like structures, often without a clear two-phase region. Intermediates in the form of disks, either micelles or bilayer fragments, have been observed in several cases. Most noteworthy are the planar and circular disks found in systems containing a large fraction of cholesterol in the bilayer. Bile salts are a special class of surfactants that seem to break down the bilayer at low additions. Originally, disk-like mixed micelles were conjectured, with polar membrane lipids building the disk, and the bile salts covering the hydrophobic rim. Later work has shown that flexible cylinders are the dominant intermediates also in these systems, even if the disk-like structures have been re-established as transients in the transformation from mixed micelles to vesicles.

Buffers↗
PubMed2002

The 40th anniversary of bilayer lipid membrane research.

This paper presents a historic perspective on the origin of the lipid bilayer concept and its experimental realization. Additionally, current studies in close collaboration with our colleagues on the use of supported BLMs as biosensors and molecular devices are delineated. Further, recent research of others on BLMs (planar lipid bilayers) is referenced.

History, 20th Century↗