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BBA - Biomembranes (v.1758, #6)

Editorial Board (pp. ii).

Electrostatic interactions of colicin E1 with the surface of Escherichia coli total lipid by Chunhong Tian; Elaine Tétreault; Christopher K. Huang; Tanya E.S. Dahms (pp. 693-701).

The surface properties of colicin E1, a 522-amino acid protein, and its interaction with monolayers of Escherichia coli ( E. coli) total lipid and 1,2-Dimyristoyl- sn-Glycero-3-Phosphocholine (DOPC) were studied using the Langmuir–Blodgett (LB) technique. Colicin E1 is amphiphilic, forming a protein monolayer at the air/buffer interface. The protein is thought to interact with the E. coli total lipid head groups through electrostatic interactions, followed by its insertion into the lipid monolayers. Supported lipid bilayers (SLBs) of E. coli total lipid and DOPC, deposited onto mica at the cell membrane equivalence pressure for E. coli and incubated with colicin E1, were imaged by contact mode atomic force microscopy (CM-AFM). Colicin E1 formed protein aggregates on DOPC SLBs, while E. coli total lipid SLB was deformed following its incubation with colicin E1. Corresponding lateral force images, along with electrostatic surface potentials for colicin E1 P190, imply a direct interaction of colicin E1 with lipid head groups facilitating their charge neutralization.

Keywords: Abbreviations; AFM; atomic force microscopy; CL; cardiolipin; CM; contact mode; DOPC; 1,2-Dimyristoyl-; sn; -Glycero-3-Phosphocholine; LB; Langmuir–Blodgett; LF; lateral force; PBS; phosphate buffer solution; PE; phosphatidylethanolamine; PG; phosphatidylglycerol; SLB; supported lipid bilayerAtomic force microscopy; Supported planar bilayer; Colicin E1; Cytotoxin; DOPC; Escherichia coli; total lipid; Langmuir–Blodgett; Monolayer; Protein–Lipid Interaction

Reciprocal inhibition of Cd²⁺ and Ca²⁺ uptake in human intestinal crypt cells for voltage-independent Zn-activated pathways by Pierre-Michel Bergeron; Catherine Jumarie (pp. 702-712).

Cadmium–Ca–Zn interactions for uptake have been studied in human intestinal crypt cells HIEC. Our results failed to demonstrate any significant cross-inhibition between Cd and Ca uptake under single metal exposure conditions. However, they revealed a strong reciprocal inhibition for a Zn-stimulated mechanism of transport. Optimal stimulation was observed under exposure conditions that favor an inward-directed Zn gradient, suggesting activation by extracellular rather than intracellular Zn. The effect of Zn on the uptake of Ca was concentration-dependent, and zinc-induced stimulation of Cd uptake resulted in a 3- and 5.8-fold increase in the K_m and V_max values, respectively. Neither basal nor Zn-stimulated Ca uptakes were sensitive to membrane depolarization. However, the stimulated component of uptake was inhibited by the trivalent cations Gd³⁺, and La³⁺ and to a lesser extent by Mg²⁺ and Ba²⁺. RT-PCR analysis as well as uptake measurement performed with extracellular ATP and/or suramin do not support the involvement of purinergic P2X receptor channels. Uptake and fluorescence data led to the conclusion that Zn is unlikely to trigger Ca influx in response to Ca release from thapsigargin-sensitive intracellular pools. Our data show that Zn may potentiate Cd accumulation in intestinal crypt cells through mechanism that still needs to be clarified.

Keywords: Cadmium; Calcium; Zinc; Intestinal crypt cell; P2XR; SOCs; CRAC; Zn-sensing receptor

Cellular uptake and subsequent intracellular trafficking of R8-liposomes introduced at low temperature by Akitada Iwasa; Hidetaka Akita; Ikramy Khalil; Kentaro Kogure; Shiroh Futaki; Hideyoshi Harashima (pp. 713-720).

Intracellular trafficking is a determining factor in the transgene expression efficiency of gene vectors. In the present study, the mechanism of the cellular uptake of octaarginine (R8)-modified liposomes, when introduced at 37 °C and 4 °C, was investigated in living cells. Compared with 37 °C, the uptake of R8-liposomes was only slightly reduced at 4 °C. Dual imaging of liposomes and plasma membranes revealed that R8-liposomes were internalized by vesicular transport, and partially escaped to the cytosol at the perinuclear region at 37 °C. When introduced at 4 °C, intracellular liposomes were observed within a specific region close to the plasma membrane, and internalization of the plasma membrane was completely inhibited. Therefore, at 4 °C, R8-liposomes appear to enter cells via unique pathway, which is separate and distinct from energy-dependent vesicular transport. The subsequent nuclear delivery of encapsulated pDNA, when introduced at 4 °C, was less prominent compared with those introduced at 37 °C. Collectively, these findings demonstrate that a vesicular transport-independent pathway is responsible for the cellular uptake of liposomes. In addition, the uptake route is closely related to the subsequent nuclear delivery process; the operation of an endogenous vesicular sorting system is advantageous for the nuclear delivery of pDNA.

Keywords: Intracellular trafficking; PTD; R8; Liposome; Cellular uptake

Structure–activity relationship study of the cell-penetrating peptide pVEC by Anna Elmquist; Mats Hansen; Ülo Langel (pp. 721-729).

The peptide pVEC is a recently described cell-penetrating peptide, derived from the murine vascular endothelial-cadherin protein. In order to define which part of this 18-amino acid long peptide is important for the cellular translocation, we performed a structure–activity relationship study of pVEC. Together with thel-alanine substituted peptides, the retro- pVEC, D- pVEC and the scramble pVEC are studied for comparison. The peptide analogues are labeled with carboxyfluorescein at the N-terminus for monitoring the cellular uptake into human Bowes melanoma cells with different efficacy. We show that all the Fl- pVEC analogues internalize in live Bowes melanoma cells.l-Alanine substitution of the five respective N-terminal hydrophobic amino acids significantly decreases the translocation property, while replacing of Arg⁶, Arg⁸ or Ser¹⁷ by alanine enhances the uptake. The uptake of pVEC is significantly reduced by treatment with an endocytosis inhibitor wortmannin. Treatment with heparinase III, nystatin and EIPA had no effect on the peptide uptake. The data presented here show that the N-terminal hydrophobic part of pVEC is crucial for efficient cellular translocation.

Keywords: Abbreviations; BMC; Bowes melanoma cells; CPP; cell-penetrating peptide; d; -; p; VEC; ent-p; VEC (all-; d; -enantiomer of; p; VEC); EIPA; 5-(N-ethyl-N-isopropyl)-amiloride; Fl; 5-(and-6) carboxyfluoresceinyl; HKR; HEPES-buffered Krebs–Ringer solution; LDH; lactate dehydrogenase; MALDI-TOF; matrix-assisted laser desorption ionization time-of-flight; PI3K; phosphatidylinositol-3-OH kinase; p; VEC; peptide vascular endothelial-cadherin; RP HPLC; reverse-phase HPLC; S.A.R.; structure–activity relationship; VE-cadherin; vascular endothelial-cadherin p; VEC; Cell-penetrating peptide; VE-cadherin; Cellular uptake; l; -Ala-scan, S.A.R study

Brownian dynamics investigation into the conductance state of the MscS channel crystal structure by Taira Vora; Ben Corry; Shin-Ho Chung (pp. 730-737).

We suggest that the crystal structure of the mechanosensitive channel of small conductance is in a minimally conductive state rather than being fully activated. Performing Brownian dynamics simulations on the crystal structure show that no ions pass through it. When simulations are conducted on just the transmembrane domain (excluding the cytoplasmic residues 128 to 280) ions are seen to pass through the channel, but the conductance of ∼ 30 pS is well below experimentally measured values. The mutation L109S that replaces a pore lining hydrophobic residue with a polar one is found to have little effect on the conductance of the channel. Widening the hydrophobic region of the pore by 2.5 Å however, increases the channel conductance to over 200 pS suggesting that only a minimal conformational change is required to gate the pore.

Keywords: MscS; Ion channel; Mechanosensation; Brownian dynamic; Electrostatic; Conductance

Molecular cloning and characterization of ouabain-insensitive Na⁺-ATPase in the parasitic protist, Trypanosoma cruzi by Kyoichi Iizumi; Yuko Mikami; Muneaki Hashimoto; Takeshi Nara; Yukichi Hara; Takashi Aoki (pp. 738-746).

Maintaining low intracellular sodium concentrations is vital for almost all organisms. Na⁺ efflux is generally governed by P-type ATPases, Na⁺/K⁺-ATPase in animals and Na⁺-ATPase, called ENA, in fungi and plants. Trypanosoma cruzi, which parasitizes mammalian cells, must undergo drastic adaptations to high Na⁺ concentrations outside and low Na⁺ concentrations inside host cells. However, T. cruzi Na⁺ efflux pumps have not been identified. We report here the cloning and characterization of the gene encoding Na⁺-ATPase in T cruzi, which resembled fungal and plant ENAs, termed TcENA. TcENA was a plasma membrane protein expressed throughout the parasite life cycle. The transcription level of TcENA was higher in insect stage epimastigotes and blood stream trypomastigotes than in intracellular amastigotes, probably reflecting the high Na⁺ concentration outside the host cells. Biochemical analysis of TcENA expressed heterologously in mammalian cells demonstrated, for the fist time, that the ATPase activity of TcENA is stimulated by both Na⁺ and K⁺ and is insensitive to ouabain, a specific inhibitor of Na⁺/K⁺-ATPases. Furthermore, epimastigotes overproducing TcENA showed increased tolerance to high Na⁺ stress. Our findings suggest that TcENA acts as a sodium pump and provide insights into the regulation of ion homeostasis in the parasitic protist.

Keywords: Trypanosoma cruzi; P-type ATPase; ENA; Ouabain; Heterologous expression; Sodium tolerance

Substrate specificity of a chimera made from Xenopus SGLT1-like protein and rabbit SGLT1 by Katsumi Nagata; Yoshio Hata (pp. 747-754).

To characterize the sugar translocation pathway of Na⁺/glucose cotransporter type 1 (SGLT1), a chimera was made by substituting the extracellular loop between transmembrane domain (TM) 12 and TM13 of Xenopus SGLT1-like protein (xSGLT1L) with the homologous region of rabbit SGLT1. The chimera was expressed in Xenopus oocytes and its transport activity was measured by the two-microelectrode voltage-clamp method. The substrate specificity of the chimera was different from those of xSGLT1L and SGLT1. In addition the chimera's apparent Michaelis–Menten constant ( K_m) for myo-inositol, 0.06 mM, was about one fourth of that of xSGLT1L, 0.25 mM, while the chimera's apparent K_m ford-glucose, 0.8 mM, was about one eighth of that of xSGLT1L, 6.3 mM. Our results suggest that the extracellular loop between TM12 and TM13 participates in the sugar transport of SGLT1.

Keywords: Xenopus; SGLT1-like protein; SGLT; SMIT; Chimera

Membrane-perturbing properties of three peptides corresponding to the ectodomain of hepatitis C virus E2 envelope protein by Beatriz Pacheco; Julián Gómez-Gutiérrez; Belén Yélamos; Carmen Delgado; Fernando Roncal; Juan P. Albar; Darrell Peterson; Francisco Gavilanes (pp. 755-763).

Based on the predicted capacity to interact with membranes at the interface, we have found three regions in the ectodomain of the hepatitis C virus envelope glycoprotein E2 (430–449, 543–560 and 603–624) with the ability to destabilize membranes. Three peptides corresponding to the sequence of these regions have been synthesized and their interaction with liposomes have been characterized. The three peptides were able to insert deeply into the hydrophobic core of negatively charged phospholipids as stated by fluorescence depolarization of the probe 1,6-diphenyl-1,3,5-hexatriene. Peptides E2_430–449 and E2_603–624 were able to induce aggregation of phosphatidylglycerol vesicles in a concentration-dependent manner both at neutral and acidic pH while peptide E2_543–560 did not induce any increase of optical density at 360 nm in the concentration range studied. The three peptides induced lipid mixing and the release of the internal contents in a dose-dependent manner when acidic phospholipids were used. Fourier transformed infrared spectroscopy indicated that the peptides adopted mainly a β-sheet conformation which is not modified by the presence of acidic phospholipids. Taken together, our results point out to the involvement of these three regions in the fusion mechanism of HCV at the plasma membrane level.

Phase diagram of stigmasterol-dipalmitoylphosphatidylcholine mixtures dispersed in excess water by Ruiguang Wu; Lin Chen; Zhiwu Yu; Peter J. Quinn (pp. 764-771).

As a simple model of rafts in plant cells, the effect of stigmasterol, one of the predominant sterols in plant plasma membranes, on the phase behavior of dipalmitoylphosphatidylcholine (DPPC) multilayers has been studied by X-ray diffraction (XRD), differential scanning calorimetry (DSC), and freeze-fracture electron microscopy (FFEM) techniques. A partial phase diagram of the binary system has been constructed. Particularly, the stigmasterol concentrations of the “left endpoint�? and “right endpoint�? of the three-phase line have been determined using the newly developed linear and nonlinear fitting method. They are 6.2 and 23.7 mol%, respectively. Furthermore, the resemblance and difference of phase diagrams of DPPC/stigmasterol, DPPC/cholesterol, and DPPC/ergosterol have been compared and the efficiency of these sterols in promoting the formation of the liquid-ordered domains (rafts) have also been discussed.

Keywords: Abbreviations; DPPC; dipalmitoylphosphatidylcholine; XRD; X-ray diffraction; DSC; differential scanning calorimetry; SAXS; small-angle X-ray scattering; WAXS; wide-angle X-ray scattering; FFEM; freeze-fracture electron microscopy; L; _β′; lamellar-gel phase; P; _β′; rippled gel phase; L; _α; liquid–crystal phase; L; _oβ; liquid-ordered phase; T; _p; the peak temperature of the sharp components of deconvoluted DSC curves; T; _end; the endpoint temperature of the broad components of deconvoluted DSC curvesStigmasterol; DPPC; Phase diagram; X-ray diffraction; DSC; Raft

The structural properties of the transmembrane segment of the integral membrane protein phospholamban utilizing¹³C CPMAS,²H, and REDOR solid-state NMR spectroscopy by Ethan S. Karp; Elvis K. Tiburu; Shadi Abu-Baker; Gary A. Lorigan (pp. 772-780).

Solid-state NMR spectroscopic techniques were used to investigate the secondary structure of the transmembrane peptide phospholamban (TM-PLB), a sarcoplasmic Ca²⁺ regulator.¹³C cross-polarization magic angle spinning spectra of¹³C carbonyl-labeled Leu39 of TM-PLB exhibited two peaks in a pure 1-palmitoyl-2-oleoyl-phosphocholine (POPC) bilayer, each due to a different structural conformation of phospholamban as characterized by the corresponding¹³C chemical shift. The addition of a negatively charged phospholipid (1-palmitoyl-2-oleoylphosphatidylglycerol (POPG)) to the POPC bilayer stabilized TM-PLB to an α-helical conformation as monitored by an enhancement of the α-helical carbonyl¹³C resonance in the corresponding NMR spectrum.¹³C–¹⁵N REDOR solid-state NMR spectroscopic experiments revealed the distance between the¹³C carbonyl carbon of Leu39 and the¹⁵N amide nitrogen of Leu42 to be 4.2±0.2Å indicating an α-helical conformation of TM-PLB with a slight deviation from an ideal 3.6 amino acid per turn helix. Finally, the quadrupolar splittings of three²H labeled leucines (Leu28, Leu39, and Leu51) incorporated in mechanically aligned DOPE/DOPC bilayers yielded an 11°±5° tilt of TM-PLB with respect to the bilayer normal. In addition to elucidating valuable TM-PLB secondary structure information, the solid-state NMR spectroscopic data indicates that the type of phospholipids and the water content play a crucial role in the secondary structure and folding of TM-PLB in a phospholipid bilayer.

Keywords: Solid-state nuclear magnetic resonance spectroscopy; Phospholamban; REDOR; Membrane protein; Transmembrane domain; ¹³; C CPMAS; Peptide tilt

Ala-504 is a determinant of substrate binding affinity in the mouse Na⁺/dicarboxylate cotransporter by Naomi Oshiro; Ana M. Pajor (pp. 781-788).

The Na⁺/dicarboxylate cotransporters from mouse (mNaDC1) and rabbit (rbNaDC1) differ in their ability to handle adipate, a six-carbon terminal dicarboxylic acid. The mNaDC1 and rbNaDC1 amino acid sequences are 75% identical. The rbNaDC1 does not transport adipate and only succinate produced inward currents under two-electrode voltage clamp. In contrast, oocytes expressing mNaDC1 had adipate-dependent inward currents that were about 60% of those induced by succinate. In order to identify domains involved in adipate transport, we examined the functional properties of a series of chimeric transporters made between mouse and rabbit NaDC1. We find that multiple transmembrane helices (TM), particularly TM 8, 9, and 10, are involved in adipate transport. In TM 10 there is only one amino acid difference between the two proteins, corresponding to Ala-504 in mouse and Ser-512 in rabbit NaDC1. The mNaDC1-A504S mutant had decreased adipate-dependent currents relative to succinate-dependent currents and an increase in the K_0.5 for both succinate and glutarate. We conclude that multiple amino acids from TM 8, 9 and 10 contribute to the transport of adipate in NaDC1. Furthermore, Ala-504 in TM 10 is an important determinant of K_0.5 for both adipate and succinate.

Keywords: Adipate; Succinate; NaDC1; Sodium; Xenopus; oocytes; Substrate specificity

Relative contribution of OAT1 and OAT3 transport activities in isolated perfused rabbit renal proximal tubules by Anusorn Lungkaphin; Buarong Lewchalermwongse; Varanuj Chatsudthipong (pp. 789-795).

The expression of both OAT1 and OAT3 along the isolated rabbit renal proximal tubule (RPT) was determined using RT-PCR. They were found to be very strong in S2 segment and weak in S1 and S3 segments. We further examined the relative transport activity of these transporters in isolated perfused rabbit RPT using [³H] para-aminohippurate ([³H]PAH), and estrone sulfate ([³H]ES) as specific substrates for rbOAT1 and rbOAT3, respectively. The transport activity of OAT1 was in the order S2>S1=S3 segments and that of OAT3 was in the order S1=S2>>S3 segments. The addition of α-ketoglutarate (100 μM) in the bathing medium increased both OAT1 and OAT3 transport activities in all segments of proximal tubule. The kinetics of [³H]succinic acid transport, used to measure the activity of sodium dicarboxylate transporter 3 (NaDC3), were examined. The J_max for succinic acid was in the order S2>S3 and unmeasurable in the S1 segment. Our data indicate that both OAT1 and OAT3 play quantitatively significant roles in the renal transport of organic anions along the proximal tubule but predominately in S2 segment. The relative contribution of both transporters depends on their relative expression levels and may possibly be affected by the activity of NaDC3 in RPT.

Keywords: Organic anion transporter 1; Organic anion transporter 3; Renal proximal tubule

Characterization and comparison of raft-like membranes isolated by two different methods from rat submandibular gland cells by Mikel García-Marcos; Stéphanie Pochet; Séverine Tandel; Unai Fontanils; Egoitz Astigarraga; José Andrés Fernández-González; Alain Kumps; Aida Marino; Jean-Paul Dehaye (pp. 796-806).

Lipid rafts are defined as cholesterol and sphingolipid enriched domains in biological membranes. Their role in signalling and other cellular processes is widely accepted but the methodology used for their biochemical isolation and characterization remains controversial. Raft-like membranes from rat submandibular glands were isolated by two different protocols commonly described in the literature; one protocol was based on selective solubilization by Triton X-100 at low temperature and the other protocol consisted in extensive sonication. In both cases a low density vesicular fraction was obtained after ultracentrifugation in a sucrose density gradient. These fractions contained about 20% of total cholesterol but less than 8% of total proteins, and were more rigid than bulk membranes. Fatty acid analyses revealed a similar composition of raft-like membranes isolated by the two different methods, which was characterized by an enrichment in saturated fatty acids in detriment of polyunsaturated acids when compared with the whole cell membranes. Protein profile of detergent resistant membranes or raft-like membranes prepared by sonication was assessed by silver staining after SDS-PAGE and by MALDI-TOF. Both analyses provided evidence of a different protein composition of the Triton X-100 and sonication preparations. Immunoblot experiments revealed that raft-like membranes prepared by detergent extraction or sonication were free of Golgi apparatus or endoplasmic reticulum protein markers (β-COP and calnexin, respectively) and that they were not substantially contaminated by transferrin receptor (a non-raft protein). While caveolin-1 was highly enriched in raft-like membranes prepared by the two methods, the P2X₇ receptor was enriched in raft-like membrane fractions prepared by sonication, but almost undetectable in the detergent resistant membranes. It can be concluded that both methods can be used to obtain raft-like membranes, but that detergent may affect protein interactions responsible for their association with different membrane domains.

Keywords: Abbreviations; MALDI-TOF; matrix assisted laser desorption ionization-time of flight; SDS-PAGE; sodium dodecyl sulphate-polyacrylamide gel electrophoresis; PUFA; polyunsaturated fatty acid; BSA; bovine serum albumin; EDTA; ethylenediaminetetraacetic acid; EGTA; ethylene glycol-bis-(β-aminoethyl ether)-; N; ,; N; ,; N′; ,; N′; -tetraacetic acid; HEPES; N; - piperazine-; N′; -[2-ethanesulfonic acid]; HBS; HEPES-buffered saline; HS; HEPES-saline; DPH; 2-[3-(diphenylhexatriene)]; PBS; phosphate-buffered saline; GC-MS; gas chromatography-mass spectrometry; TfR; transferrin receptor; CNX; calnexin; COP; coatomer proteinMembrane microdomains; Triton X-100; purinergic receptors; mass spectrometry; P2X; ₇

Molecular features of phospholipids that affect glycolipid transfer protein-mediated galactosylceramide transfer between vesicles by Matts Nylund; Matti A. Kjellberg; Julian G. Molotkovsky; Hoe-Sup Byun; Robert Bittman; Peter Mattjus (pp. 807-812).

The glycolipid transfer protein (GLTP)-mediated movement of galactosylceramide from model membrane donor vesicles to acceptor vesicles is sensitive to the membrane environment surrounding the glycolipid. GLTP can catalyze the transfer of a fluorescently labeled GSL, anthrylvinyl-galactosylceramide (AV-GalCer), from vesicles composed of 1-palmitoyl-2-oleoyl- sn-glycero-3-phosphocholine and dipalmitoylphosphatidylcholine matrices, but not from vesicles prepared from N-palmitoylsphingomyelin, regardless of the cholesterol content of the vesicles. In this study, we have examined the structural features of sphingomyelin (SM) that are responsible for its inhibition of the rate of GLTP-catalyzed transfer of AV-GalCer. The rate of glycolipid transfer was enhanced when the N-palmitoyl chain of SM was replaced with an N-oleoyl chain. Analogs of N-palmitoyl-SM in which the 4,5-double bond of the long-chain base is reduced or the 3-hydroxy group is removed did not inhibit GLTP-catalyzed transfer of AV-GalCer. When the donor vesicles were prepared with phosphatidylcholines or ether-linked phosphatidylcholine analogs, the transfer rates of AV-GalCer increased with increasing degree of unsaturation. The rate of AV-GalCer transfer was strongly dependent on the unsaturation degree of the acyl and/or alkyl chains. For ester-linked PCs, the transfer rate increased in the order DPPCcis double bonds, respectively.

Keywords: Abbreviations; SUV; small unilamellar vesicles; GLTP; glycolipid transfer protein; GSL; glycosphingolipids; PSM; N; -palmitoyl-; d; -; erythro-; sphingosylphosphorylcholine; PDHSM; N; -palmitoyl-; d; -; erythro-; dihydrosphingosylphosphorylcholine; OSM; N; -oleoyl-; d; -; erythro-; sphingosylphosphorylcholine; ODHSM; N; -oleoyl-; d; -; erythro-; dihydrosphingosylphosphorylcholine; 3-deoxy-PSM; 3-deoxy-; N; -palmitoylsphingosylphosphorylcholine; POPC; 1-palmitoyl-2-oleoyl-; sn; -glycero-3-phosphocholine; DPPC; 1,2-dipalmitoyl-; sn; -glycero-3-phosphocholine; DOPC; 1,2-dioleoyl-; sn; -glycero-3-phosphocholine; HPPC; 1-; O; -hexadecyl-2-(deoxy-; N; -palmitoylamido)-; sn; -glycero-3-phosphocholine; DHPC; 1,2-di-; O; -hexadecyl-; sn; -glycero-3-phosphocholine; di-oleyl-PC; 1,2-di-; O; -octadec-9(; Z; )-enyl-; sn; -glycero-3-phosphocholine; HOPC; 1-; O; -hexadecyl-2-oleoyl-; sn; -glycero-3-phosphocholine; AV-GalCer; N; -[(11; E; )-12-(9-anthroyl)-11-dodecenoyl]-1-; O; -β-galactosylsphingosine; DiOC; ₁₆; 3,3′-dihexadecyloxacarbocyanine perchlorateSphingomyelin; Phosphatidylcholine; Fluorescence; glycosphingolipid; Cholesterol; Glycolipid transfer protein; Sphingomyelin analog; Ether lipid

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BBA - Biomembranes (v.1758, #6)