The structure of a lipid–water lamellar phase containing two types of lipid monolayers. An X-ray and neutron scattering study

Ranck, Jean-Luc; Zaccai, G.; Luzzati, Vittorio

doi:10.1107/s0021889880012678

Cited by 9 publications

(25 citation statements)

References 9 publications

(12 reference statements)

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“…the other corresponded to a lamellar repeating distance, which is about twice the La dimension having numerous small-angle reflections, h = 2, 3, 4, 5, 6, 7, 8, 9, 10 (h = 1 is absent or undetectable) and one wide-angle reflection at 4.11 A typical of stiff (B chains and a diffusion band. This unambiguously indicates the existence of an L-y lamellar phase, which consists of a two-bilayer motif composed of monolayers with stiff chains alternating with monolayers with disordered chains (Ranck et al, 1980) (Fig. 2).…”

Section: X-ray Diffractionmentioning

confidence: 83%

“…This phase is quite unusual; it has been found by x-ray scattering in the mitochondrial lipid-water system in a narrow range of temperature and at low water content (Gulik-Krzywicki et al, 1967). It has also been studied by neutron scattering (Ranck et al, 1980). The structure consists of two bilayers, each one formed by an a and a 13 monolayer (Fig.…”

Section: Discussionmentioning

confidence: 99%

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A conformation transition of lung surfactant lipids probably involved in respiration

Gulik¹,

Tchoreloff²,

Proust³

1994

Biophysical Journal

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X-ray scattering and freeze-fracture electron microscopy of a lung surfactant extract show the existence of a complex lamellar phase, L gamma, over a wide range of concentrations and temperatures. This lamellar phase, which consists of two bilayer motifs comprised of monolayers with stiff chains alternating with monolayers with disordered chains, allows us to propose a structural model of a collapse phase at the alveolar pulmonary interface. This model accounts for the increase in surface pressure during the compression as well as the easy respreading upon expansion of the interface during the respiratory cycle.

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Section: X-ray Diffractionmentioning

confidence: 83%

Section: Discussionmentioning

confidence: 99%

A conformation transition of lung surfactant lipids probably involved in respiration

Gulik¹,

Tchoreloff²,

Proust³

1994

Biophysical Journal

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“…The formation of MLP was recently observed in lipid systems consisting of 6-hydroxysphingosine-Cer 9 , sphingosine-Cer 22 , and their mixture 10 . We assume that the principles of the organization of MLP are similar to Lγ phase with asymmetric bilayers described for phospholipids [65][66][67][68] and to oriented fatty acid bilayers with well-defined asymmetric distribution of lipids 57 . MLP contains most likely an asymmetric unit arranged so that it provides the repeat distance over 10 nm 22 .…”

Section: -Deoxy-cermentioning

confidence: 99%

Behavior of 1-Deoxy-, 3-Deoxy- and N-Methyl-Ceramides in Skin Barrier Lipid Models

Kováčik

Pullmannová

Pavlíková

et al. 2020

Sci Rep

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Ceramides (Cer) are essential components of the skin permeability barrier. To probe the role of Cer polar head groups involved in the interfacial hydrogen bonding, the N-lignoceroyl sphingosine polar head was modified by removing the hydroxyls in C-1 (1-deoxy-Cer) or C-3 positions (3-deoxy-Cer) and by Nmethylation of amide group (N-Me-Cer). Multilamellar skin lipid models were prepared as equimolar mixtures of Cer, lignoceric acid and cholesterol, with 5 wt% cholesteryl sulfate. In the 1-deoxy-Cerbased models, the lipid species were separated into highly ordered domains (as found by X-ray diffraction and infrared spectroscopy) resulting in similar water loss but 4-5-fold higher permeability to model substances compared to control with natural Cer. In contrast, 3-deoxy-Cer did not change lipid chain order but promoted the formation of a well-organized structure with a 10.8 nm repeat period. Yet both lipid models comprising deoxy-Cer had similar permeabilities to all markers. N-Methylation of Cer decreased lipid chain order, led to phase separation, and improved cholesterol miscibility in the lipid membranes, resulting in 3-fold increased water loss and 10-fold increased permeability to model compounds compared to control. Thus, the C-1 and C-3 hydroxyls and amide group, which are common to all Cer subclasses, considerably affect lipid miscibility and chain order, formation of periodical nanostructures, and permeability of the skin barrier lipid models. Mammalian skin protects the body from external threats, such as chemicals and ultraviolet light, and prevents excessive water loss. The major skin permeability barrier is located in the outermost layer of the epidermis, the stratum corneum (SC) 1-3. The SC consists of corneocytes, epidermal cells in a terminal phase of differentiation, and extracellular lipid matrix, which is a multilamellar assembly of ceramides (Cer), free fatty acids and cholesterol (Chol) in an approximately 1:1:1 molar ratio, and minor components, such as cholesteryl sulfate (CholS) 1-3. Cer, i.e., N-acyl sphingosines, are simple sphingolipids that have from two to four hydroxyl groups and monosubstituted amide group, which behave as hydrogen bond donors and acceptors and affect Cer interactions with proteins and other lipids. For example, 1-deoxy-Cer do not mix well with other lipids 4 , removal of C-3 hydroxyl in Cer prevents the formation of water-extended cooperative H-bond network of Cer 5 , and Cer amide group appears to be fundamental in creating the signal-transducing membrane platforms 6. In the skin barrier, additional hydroxyls in Cer at C-4 (phytosphingosine Cer) or C-6 positions (6-hydroxyCer) modulate the lipid miscibility, lamellar arrangement and permeability of model SC lipid mixtures 7-10 , along with the correct acyl chain length 11,12 or sphingosine chain length of Cer 13,14. Topical supplementation of skin lipids in diseases such as atopic dermatitis or ichthyoses is an established therapeutic approach. Such Cer-dominant lipids are safe, can actually prevent inflammation in...

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“…The answer is yes. Luzzati and collaborators (4–6) described several phases consisting of mixed bilayers with one monolayer of type α (disordered chains) and the other of type β (ordered chains). Figure 2a shows a phase reported for egg lecithin or phosphatidic acid in water denominated L αβ , which consists of disordered mosaics of two types of domains where monolayers α and β can be randomly associated (4).…”

Section: Can Lipids In the Different Leaflets Of A Bilayer Be Maintaimentioning

confidence: 99%

“…Figure 2a shows a phase reported for egg lecithin or phosphatidic acid in water denominated L αβ , which consists of disordered mosaics of two types of domains where monolayers α and β can be randomly associated (4). Bilayers of Lγ phase of type II obtained with mitochondrial lipids are also mixed with one monolayer of type α and one monolayer of type β (5). Thus asymmetric lateral domains, with alternative fluid and ordered regions, can be formed even with a single lipid component at thermal equilibrium.…”

Section: Can Lipids In the Different Leaflets Of A Bilayer Be Maintaimentioning

confidence: 99%

Transmembrane Asymmetry and Lateral Domains in Biological Membranes

Devaux

Morris

2004

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244

193

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It is generally assumed that rafts exist in both the external and internal leaflets of the membrane, and that they overlap so that they are coupled functionally and structurally. However, the two monolayers of the plasma membrane of eukaryotic cells have different chemical compositions. This out‐of‐equilibrium situation is maintained by the activity of lipid translocases, which compensate for the slow spontaneous transverse diffusion of lipids. Thus rafts in the outer leaflet, corresponding to domains enriched in sphingomyelin and cholesterol, cannot be mirrored in the inner cytoplasmic leaflet. The extent to which lipids contribute to raft properties can be conveniently studied in giant unilamellar vesicles. In these, cholesterol can be seen to condense with saturated sphingolipids or phosphatidylcholine to form μm scale domains. However, such rafts fail to model biological rafts because they are symmetric, and because their membranes lack the mechanism that establishes this asymmetry, namely proteins. Biological rafts are in general of nm scale, and almost certainly differ in size and stability in inner and outer monolayers. Any coupling between rafts in the two leaflets, should it occur, is probably transient and dependent not upon the properties of lipids, but on transmembrane proteins within the rafts.

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The structure of a lipid–water lamellar phase containing two types of lipid monolayers. An X-ray and neutron scattering study

Cited by 9 publications

References 9 publications

A conformation transition of lung surfactant lipids probably involved in respiration

A conformation transition of lung surfactant lipids probably involved in respiration

Behavior of 1-Deoxy-, 3-Deoxy- and N-Methyl-Ceramides in Skin Barrier Lipid Models

Transmembrane Asymmetry and Lateral Domains in Biological Membranes

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