Spontaneous domain formation of phospholipase A2 at interfaces: Fluorescence microscopy of the interaction of phospholipase A2 with mixed monolayers of lecithin, lysolecithin and fatty acid

Reichert, A.; Ringsdorf, Helmut; Wagenknecht, A. C.

doi:10.1016/0005-2736(92)90237-g

Cited by 42 publications

(40 citation statements)

References 58 publications

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“…21 Additional studies have reported that bound PLA 2 molecules tend to preferentially accumulate at boundaries between lipid phases. [33][34][35] We note here that during imaging of the optical textures of 5CB upon specific binding of PLA 2 to D-DPPC, we were able to resolve domains in the LC by transmission of either polarized light ( Figure 4A) or light without a preferred polarization ( Figure 4B). Upon heating of 5CB into its isotropic phase (>35°C), the appearance of the 5CB became uniformly dark between crossed polarizers ( Figure 4C) and uniformly bright in the absence of polarizers ( Figure 4D).…”

Section: Resultsmentioning

confidence: 95%

“…Past studies have reported that hydrolysis of L-DPPC causes the formation of phase-separated domains of the acid product and L-DPPC. 33,34,51 We speculate that the inhomogeneous distribution of the TR-DPPE and the orientation of the LC reflect the accumulation of the hydrolysis products of L-DPPC, especially palmitic acid, in spatially localized regions of the interface.…”

Section: Resultsmentioning

confidence: 98%

“…33,34 We sought to find evident of this association by using fluorescently labeled PLA 2 (PLA 2 -488). However, we observed no significant fluorescence activity when using 1 nM of PLA 2 .…”

Section: Resultsmentioning

confidence: 99%

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Coupling of the Orientations of Thermotropic Liquid Crystals to Protein Binding Events at Lipid-Decorated Interfaces

2007

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We report a study of the interactions of proteins with monolayers of phospholipids (D/L-alpha-dipalmitoyl phosphatidylcholine and L-alpha-dilauroyl phosphatidylcholine) spontaneously assembled at an interface between an aqueous phase and a 20-microm-thick film of a nematic liquid crystal (4'-pentyl-4-cyanobiphenyl). Because the orientation of the liquid crystal is coupled to the organization of the lipids, specific interactions between phospholipase A2 and the lipids (binding and/or hydrolysis) that lead to reorganization of the lipids are optically reported (using polarized light) as dynamic orientational transitions in the liquid crystal. In contrast, nonspecific interactions between proteins such as albumin, lysozyme, and cytochrome-c and the lipid-laden interface of the liquid crystal are not reported as orientational transitions in the liquid crystals. Concurrent epifluorescence and polarized light imaging of labeled lipids and proteins at the aqueous-liquid crystal interface demonstrate that spatially patterned orientations of the liquid crystals observed during specific binding of phospholipase A2 to the interface, as well as during the subsequent hydrolysis of lipids by phospholipase A2, reflect the lateral organization (micrometer-sized domains) of the proteins and lipids, respectively, at the aqueous-liquid crystal interface.

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Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 98%

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Coupling of the Orientations of Thermotropic Liquid Crystals to Protein Binding Events at Lipid-Decorated Interfaces

2007

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“…They all catalyze stereospecifically the hydrolytic cleavage of ester linkages of the 2-acyl group (hence the designation A 2 ) of membrane-forming glycerophospholipids to release the corresponding lysophospholipids and free fatty acids. Its importance in many biological processes like rebuilding and modification of membranes and release of arachidonic acid, together with its clear preference for interfaces of organized substrate aggregates in aqueous dispersions as monolayers, bilayers, and micelles, has produced an overwhelming amount of information about its enzymatic action (4,32,33). A schematic diagram of this interfacial catalysis is given in Fig.…”

Section: Variable Load: Interfacial Hydrolysis Of Phospholipids Monolmentioning

confidence: 99%

Development of a Constant Surface Pressure Penetration Langmuir Balance Based on Axisymmetric Drop Shape Analysis

Wege

Holgado-Terriza

Cabrerizo-Vílchez

2002

Journal of Colloid and Interface Science

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“…Specifically, by using grazing incidence x-ray diffraction, it was shown that specific binding of the protein phospholipase A 2 (PLA 2 ) to d -DPPC leads to reorganization of the lipid tails of the d -DPPC within a monolayer at the surface of an aqueous phase. 68, 69 In contrast, addition of a protein that does not bind d -DPPC, such as BSA, did not trigger the ordering transition within the d -DPPC lipid monolayer. Recent studies have demonstrated that such protein-induced reorganization of lipid monolayers (caused by specific binding events) can trigger ordering transitions in LC films decorated with the lipids.…”

Section: Approaches To Interfacial Design Of Lc Materials For Biologimentioning

confidence: 97%

Liquid Crystalline Materials for Biological Applications

2011

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Liquid crystals have a long history of use as materials that respond to external stimuli (e.g., electrical and optical fields). More recently, a series of investigations have reported the design of liquid crystalline materials that undergo ordering transitions in response to a range of biological interactions, including interactions involving proteins, nucleic acids, viruses, bacteria and mammalian cells. A central challenge underlying the design of liquid crystalline materials for such applications is the tailoring of the interface of the materials so as to couple targeted biological interactions to ordering transitions. This review describes recent progress toward design of interfaces of liquid crystalline materials that are suitable for biological applications. Approaches addressed in this review include the use of lipid assemblies, polymeric membranes containing oligopeptides, cationic surfactant-DNA complexes, peptide-amphiphiles, interfacial protein assemblies and multi-layer polymeric films.

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Spontaneous domain formation of phospholipase A2 at interfaces: Fluorescence microscopy of the interaction of phospholipase A2 with mixed monolayers of lecithin, lysolecithin and fatty acid

Cited by 42 publications

References 58 publications

Coupling of the Orientations of Thermotropic Liquid Crystals to Protein Binding Events at Lipid-Decorated Interfaces

Coupling of the Orientations of Thermotropic Liquid Crystals to Protein Binding Events at Lipid-Decorated Interfaces

Development of a Constant Surface Pressure Penetration Langmuir Balance Based on Axisymmetric Drop Shape Analysis

Liquid Crystalline Materials for Biological Applications

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