Passive ion permeability of lipid membranes modelled via lipid-domain interfacial area

Cruzeiro, Leonor; Mouritsen, Ole G.

doi:10.1016/0005-2736(88)90316-1

Cited by 178 publications

(115 citation statements)

References 37 publications

Supporting

Mentioning

111

Contrasting

Unclassified

Order By: Relevance

“…It is well established that the defects stimulate ion permeability (37,38) and the rate of flip-flop of PLs (39). Similarly, the microsolubilization of multilamellar vesicles of dimyristoylphosphatidylcholine by apoA-I is accelerated at the T M (?24jC), at which the gel and L d phases coexist and lattice defects occur (40)(41)(42).…”

Section: Discussionmentioning

confidence: 99%

Spontaneous reconstitution of discoidal HDL from sphingomyelin-containing model membranes by apolipoprotein A-I

Fukuda

Nakano

Sriwongsitanont

et al. 2007

Journal of Lipid Research

View full text Add to dashboard Cite

Nascent HDL is known to be formed by the interaction of apolipoprotein A-I (apoA-I) with transmembrane ABCA1, but the molecular mechanism by which nascent HDL forms is less well understood. Here, we studied how reconstituted high density lipoprotein (rHDL) forms spontaneously on the interaction of apoA-I with model membranes. The formation of rHDL from pure phosphatidylcholine (PC) large unilamellar vesicles (LUVs) proceeded very slowly at 37.0jC, but sphingomyelin (SM) -rich PC/SM LUVs, which are in a gel/liquid-disordered phase (L d phase) at this temperature, were rapidly microsolubilized to form rHDL by apoA-I. The addition of cholesterol decreased the rate at which rHDL formed and induced the selective extraction of lipids by apoA-I, which preferably extracted lipids of L d phase rather than lipids of liquid-ordered phase. In addition, apoA-I extracted lipids from the outer and inner leaflets of LUVs simultaneously. These results suggest that the heterogeneous interface of the mixed membranes facilitates the insertion of apoA-I and induces L d phase-selective but leaflet-nonselective lipid extraction to form rHDL; they are compatible with recent cell works on apoA-I-dependent HDL generation.-Fukuda, M., M. Nakano, S. Sriwongsitanont, M. Ueno, Y. Kuroda, and T. Handa. Spontaneous reconstitution of discoidal HDL from sphingomyelin-containing model membranes by apolipoprotein A-I. J. Lipid Res. 2007. 48: 882-889.

show abstract

Section: Discussionmentioning

confidence: 99%

Spontaneous reconstitution of discoidal HDL from sphingomyelin-containing model membranes by apolipoprotein A-I

Fukuda

Nakano

Sriwongsitanont

et al. 2007

Journal of Lipid Research

View full text Add to dashboard Cite

show abstract

“…This is reminiscent of the morphology of a membrane at the phase-transition temperature. At the interfacial regions between the phospholipids and the P(3-HB) crystallites, discrete current fluctuations could occur, when a certain voltage is applied, similar to the phenomena observed for phospholipid bilayers at their phase-transition temperature [24] [26] [27]. At this point of our investigation, this is a speculative model which is being tested by further experiments.…”

mentioning

confidence: 82%

Channel‐Forming Activity of 3‐Hydroxybutanoic‐Acid Oligomers in Planar Lipid Bilayers

Seebàch¹,

Brunner

Büger

et al. 1996

Helvetica Chimica Acta

View full text Add to dashboard Cite

Dedicated to Prof. Dr. Edgar Heilbronner on the occasion of his 75th birthday (30.X.95)Monodisperse and polydisperse oligomers and polymers of 3-hydroxybutanoic acid (3-HB) containing 8, 16, ca. 28,32, ca. 60,64,96, and ca. 3000 monomer units were incorporated into palmitoyl-oleoyl-phosphatidyl choline (POPC) planar bilayers. At concentrations of 0.1-5% of oligo(3-HB), the resulting phospholipid bilayers showed typical single-channel behavior for Rb+ and Ba2+ ions, using the patch clamp technique. Thus, channel-forming activity of a pure polyester has been demonstrated for the first time (Figs. I, 3, and 6 ) . Single-channel activity depends upon the following structural parameters of the 3-HB derivatives: unprotected OH and COOH groups on the chain ends; chain length 2 16 monomer units; no high-molecular-weight as in P(3-HB). The results are discussed in view of the Ca2+-specific channel formed with the P(3-HP)/Ca .PP, complex from genetically competent Escherichiu coli and in view of the ubiquitous occurrence of low-molecular-weight P(3-HB) in prokaryotic and eukaryotic organisms. A simple model for the channel-causing structure is proposed, based on the proven tendency of oligo-and poly(3-HB) to form ca. 50-8, thick lamellar crystallites.

show abstract

“…2B) (16). Phase segregation of lipids has been proposed to cause phase-boundary defects leading to membrane permeabilization (72)(73)(74)(75), and it has been speculated that hydrophobic mismatches at the interface between fluid (thinner) and rigid (thicker) lipid domains compromise the barrier capacity of membranes (76). Transitions between the fluid lipid-daptomycin clusters (rigidified through tight clustering of fluid, short-chain lipids) and the more rigid (thicker) bulk of the cell membrane likely constitute such weak spots through which proton leakage can occur and might explain the gradual depolarization of the membrane.…”

Section: Discussionmentioning

confidence: 99%

Daptomycin inhibits cell envelope synthesis by interfering with fluid membrane microdomains

Müller

Wenzel

Strahl

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

380

506

View full text Add to dashboard Cite

Daptomycin is a highly efficient last-resort antibiotic that targets the bacterial cell membrane. Despite its clinical importance, the exact mechanism by which daptomycin kills bacteria is not fully understood. Different experiments have led to different models, including (i) blockage of cell wall synthesis, (ii) membrane pore formation, and (iii) the generation of altered membrane curvature leading to aberrant recruitment of proteins. To determine which model is correct, we carried out a comprehensive mode-of-action study using the model organism Bacillus subtilis and different assays, including proteomics, ionomics, and fluorescence light microscopy. We found that daptomycin causes a gradual decrease in membrane potential but does not form discrete membrane pores. Although we found no evidence for altered membrane curvature, we confirmed that daptomycin inhibits cell wall synthesis. Interestingly, using different fluorescent lipid probes, we showed that binding of daptomycin led to a drastic rearrangement of fluid lipid domains, affecting overall membrane fluidity. Importantly, these changes resulted in the rapid detachment of the membrane-associated lipid II synthase MurG and the phospholipid synthase PlsX. Both proteins preferentially colocalize with fluid membrane microdomains. Delocalization of these proteins presumably is a key reason why daptomycin blocks cell wall synthesis. Finally, clustering of fluid lipids by daptomycin likely causes hydrophobic mismatches between fluid and more rigid membrane areas. This mismatch can facilitate proton leakage and may explain the gradual membrane depolarization observed with daptomycin. Targeting of fluid lipid domains has not been described before for antibiotics and adds another dimension to our understanding of membrane-active antibiotics.antibiotics | daptomycin | membrane potential | cell wall biosynthesis | Bacillus subtilis

show abstract

Passive ion permeability of lipid membranes modelled via lipid-domain interfacial area

Cited by 178 publications

References 37 publications

Spontaneous reconstitution of discoidal HDL from sphingomyelin-containing model membranes by apolipoprotein A-I

Spontaneous reconstitution of discoidal HDL from sphingomyelin-containing model membranes by apolipoprotein A-I

Channel‐Forming Activity of 3‐Hydroxybutanoic‐Acid Oligomers in Planar Lipid Bilayers

Daptomycin inhibits cell envelope synthesis by interfering with fluid membrane microdomains

Contact Info

Product

Resources

About