Lipid-specific fluorescent probes in studies of biological membranes

Bergel'son, L. D.; Molotkovsky, Jul.G.; Manevich, Yefim

doi:10.1016/0009-3084(85)90083-0

Cited by 57 publications

(29 citation statements)

References 65 publications

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“…Such features endow the Me 4 -BODIPY-8 fluorophore with obvious advantages over other fluorophores, such as unsymmetrical, dimethylated BODIPYs, NBD (1), or perylene (5). By embedding in the bilayer to the maximal depth allowed by the linking acyl chain, the Me 4 -BODIPY-8 fluorophore is expected to be particularly useful for studies in which fluorophore localization in the membrane is needed (e.g., studies of membrane topography involving protein-lipid interactions).…”

Section: Discussionmentioning

confidence: 99%

“…1-Acyl-2-[12-(9-anthryl)-11E-dodecenoyl]-sn-glycero-3-phosphocholine (AV12-PC; Fig. 1) was prepared as described previously (5). Other phosphatidylcholines were from Avanti Polar Lipids (Alabaster, AL).…”

Section: Methodsmentioning

confidence: 99%

“…The first probe set designed to achieve this goal was a series of n-(9-anthroyloxy) fatty acids synthesized by Thulborn and Sawyer (4), who showed that the fluorophore resided in the bilayer at a graded series of depths that coincided with the attachment point of the anthroyloxy fluorophore along the acyl chain. Other widely used fluorophores, such as N-dansyl (5) or N-NBD (6, 7), have been shown to have polar characteristics that interfere with localization deep inside the bilayer even when attached to the end of the acyl chain.…”

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confidence: 99%

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New BODIPY lipid probes for fluorescence studies of membranes

Болдырев

Zhai

Momsen

et al. 2007

Journal of Lipid Research

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Many fluorescent lipid probes tend to loop back to the membrane interface when attached to a lipid acyl chain rather than embedding deeply into the bilayer. To achieve maximum embedding of BODIPY (4,4-difluoro-4-bora-3a,4a-diaza-s-indacene) fluorophore into the bilayer apolar region, a series of sn-2 acyl-labeled phosphatidylcholines was synthesized bearing 4,4-difluoro-1,3,5,7-tetramethyl-4-bora-3a,4a-diaza-s-indacene-8-yl (Me 4 -BODIPY-8) at the end of C 3 -, C 5 -, C 7 -, or C 9 -acyl. A strategy was used of symmetrically dispersing the methyl groups at BODIPY ring positions 1, 3, 5, and 7 to decrease fluorophore polarity. Iodide quenching of the phosphatidylcholine probes in bilayer vesicles confirmed that the Me 4 -BODIPY-8 fluorophore was embedded in the bilayer. Parallax analysis of Me 4 -BODIPY-8 fluorescence quenching by phosphatidylcholines containing iodide at different positions along the sn-2 acyl chain indicated that the penetration depth of Me 4 -BODIPY-8 into the bilayer was determined by the length of the linking acyl chain. Evaluation using monolayers showed minimal perturbation of ,10 mol% probe in fluid-phase and cholesterol-enriched phosphatidylcholine. Spectral characterization in monolayers and bilayers confirmed the retention of many features of other BODIPY derivatives (i.e., absorption and emission wavelength maxima near 498 nm and ?506-515 nm) but also showed the absence of the 620-630 nm peak associated with BODIPY dimer fluorescence and the presence of a 570 nm emission shoulder at high Me 4 -BODIPY-8 surface concentrations. We conclude that the new probes should have versatile utility in membrane studies, especially when precise location of the reporter group is needed. Fluorescent lipid probes have proven to be valuable tools in membrane studies (see Ref. 1 for review). Because the determination of depth-dependent parameters of bilayers can benefit the understanding of membranous structures (2), sets of probes bearing the same fluorophore at different distances from the bilayer surface are potentially quite useful. Ideally, such fluorophores should be apolar enough to localize at the membrane depth that reflects the apolar nature of the surrounding acyl chain region without being strongly influenced by the transbilayer polarity gradient (3). The first probe set designed to achieve this goal was a series of n-(9-anthroyloxy) fatty acids synthesized by Thulborn and Sawyer (4), who showed that the fluorophore resided in the bilayer at a graded series of depths that coincided with the attachment point of the anthroyloxy fluorophore along the acyl chain. Other widely used fluorophores, such as N-dansyl (5) or N-NBD (6, 7), have been shown to have polar characteristics that interfere with localization deep inside the bilayer even when attached to the end of the acyl chain.During the past decade, BODIPY (4,4-difluoro-4-bora3a,4a-diaza-s-indacene) fluorophore probes have found a wide range of applications in cell biology and biophysics, even though this zwitterionic fluorophore wa...

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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New BODIPY lipid probes for fluorescence studies of membranes

Болдырев

Zhai

Momsen

et al. 2007

Journal of Lipid Research

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“…As was shown previously these phospholipid probes reflect the state of their natural prototypes in artificial and biological membranes (reviewed in [24]). In the present study changes in the fluidity of the microenvironment of ALauSphPCho and acylALauGroPCho incorporated into the virus membrane were monitored by measuring the steadystate fluorescence polarization, which depends inversely on the mobility of the fluorophore.…”

Section: Discussionmentioning

confidence: 60%

Interaction of influenza virus with gangliosides and liposomes containing gangliosides

Slepushkin

Starov

Bukrinskaya

et al. 1988

European Journal of Biochemistry

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It has already been shown that influenza virus binds unspecifically to liposomes containing ganglioside GM1 whereas with gangliosides G D l b and G,,, binding occurs in a specific and saturable manner [Slepushkin et al. (1986) Biol. Membr. 3,229 -2351. In the present study the mode of interaction between influenza virus and various gangliosides or phospholipid liposomes containing cholesterol and gangliosides has been investigated.The influence of exogenous gangliosides on the structure of the viral envelope was studied using fluorescent and photoactivatable phospholipids incorporated into the viral membrane. With both types of probes maximal effects of gangliosides were caused by GT1b. Addition of that ganglioside resulted in a marked decrease in the fluorescence polarization (P) of fluorescent labeled virus as well as in substantial changes in the binding of photoactivatable analogues of sphingomyelin and phosphatidylcholine to virus proteins, mainly hemagglutinin.The effects of GTlb and GDlb on P value were comparable, whereas gangliosides with other oligosaccharide chains caused much smaller changes in P. Furthermore GTlb but not Gllll influenced phospholipid-hemagglutinin crosslinking.Interaction of the virus with large unilamellar liposomes was monitored by two fluorescence assays based on resonance-energy transfer from the tryptophans and tyrosines of viral proteins to vesicles labeled with a triacylglycerol (anthrylvinyldioleoyIglycero1) or from these labeled vesicles to virions labeled with a perylenoyl derivative of galactosylcerebroside (PGalSph). A third fluorescence assay was based on relief of self-quenching in PGalSph-labeled virions, upon low-pH-induced virus-liposome fusion. With all three fusion assays the changes of fluorescence caused by GTlb were more pronounced than those induced by GM1. On the other hand, virus-

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“…However, in heterogeneous lipid matrixes where macro-or microscopic phase seggrcgations are possible, these values may differ significantly because the AV-labeled lipids tend to partition between different domains localizing predominantly together with their natural prototypes having the same head group [5,6]. Accordingly we suggested the following approach to visualize changes in lipid domain organization [5]. Membranes or cells are labeled separately with two or more AV-lipids identical or very similar in all aspects except the polar head groups.…”

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confidence: 99%

Lipid domain reorganization and receptor events Results obtained with new fluorescent lipid probes

Bergel'son¹

1992

FEBS Letters

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Binding of a ligand to the extracellular site of a membrane receptor involves conformational changes not only of the extracellular and cytoplasmic sites but also of the membrane-spanning segments of the receptor protein. The lipids forming the environment of the trans-membrane receptor segments, being flexible and mobile, must follow the shape changes of the receptor molecule to some extent. For this reason ligandreceptor binding itself can be expected to result in changes of the packing of lipid molecules surrounding the receptor. Since lipids are organized in a cooperative manner such changes may affect large areas of the membrane and hence can be registered by physical methods. It has been stated repeatedly that binding of various ligands including hormones, antibodies or lectins to membrane-associated receptors is accompanied by fluidity changes of the target membrane [1][2][3].The aim of this article is to summarize recent evidence suggesting that in highly heterogeneous biological membranes containing numerous metastable lipid domains and/or clusters conformational changes of membrane-associated proteins may result not only in global fluidity changes but also in alterations of the supramolecular lipid domain organization. Frequently such changes can be tbllowed by using, as fluorescent probe, analogs of natural membrane phospholipids or glycolipids bearing, at the end of one of the fatty acyl chains, a 9.anthrylvinyl (AV) group ( cells, and in the latter case may reside for a relatively long time in the plasma membrane without internalization [7].In comparison to most other fluorophores used in membrane research, the AV group displays important advantages. It causes little disturbance because it is nonpolar, flat, and relatively compact. When attached to the fatty acyl chain at an appropriate distance from the head group the AV-fluorophores reside uniformly and exclusively in the center of the bilayer where the host lipids are packed most loosely, and affect neither the mobility nor the orientation and conformation of the major part of the molecules of the surrounding host lipids including their head groups [8]. The AV-group is characterized also by high quantum yields and very short fluorescence lifetimes [9]. The latter property makes the AV-fluorophore suitable for fluorescence polarization measurements. Moreover, in phospholipid bilayers the restricted rotational diffusion of the AVlabeled lipid molecules is of the same time scale as the fluorescence decay. Therefore even subtle changes in the fluidity of the probes microenvironment produce considerable changes in the polarization of fluorescence. The fluorescent parameters of the AV-group (,~ 365 nm, A,~m 430 rim; high extinction coefficient) make it also a highly efficient acceptor for resonance energy transfer (RET) from nearby tryptophans. Since the distance that RET can occur over is as long as 5 nm while RET efficiency depends on the sixth power of the donoracceptor distance, RET measurements with AV-labeled lipids permits the following of even e...

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Lipid-specific fluorescent probes in studies of biological membranes

Cited by 57 publications

References 65 publications

New BODIPY lipid probes for fluorescence studies of membranes

New BODIPY lipid probes for fluorescence studies of membranes

Interaction of influenza virus with gangliosides and liposomes containing gangliosides

Lipid domain reorganization and receptor events Results obtained with new fluorescent lipid probes

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