Design of Supported Membranes Tethered via Metal-Affinity Ligand-Receptor Pairs

Rädler, Ulf; Mack, Jürgen; Persike, Norbert; Jung, Günther; Tampé, Robert

doi:10.1016/s0006-3495(00)76548-9

Cited by 45 publications

(39 citation statements)

References 41 publications

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“…Commonly employed tags include GST, HSV, FLAG, 6×His, etc. Metal cocoordinating groups such as iminodiacetic acid (IDA) and nitrilotriacetic acid (NTA) have been widely employed for direct immobilization of 6×His and 10×His tagged receptors [45,46,47,48]. The moderate affinity of the ChelateNi ++ -Histidine ternary interaction means that there is sometimes considerable decay in the level of immobilized receptor.…”

Section: Surface Chemistrymentioning

confidence: 99%

Label-free screening of bio-molecular interactions

Cooper

2003

Analytical and Bioanalytical Chemistry

414

308

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The majority of techniques currently employed to interrogate a biomolecular interaction require some type of radio- or enzymatic- or fluorescent-labelling to report the binding event. However, there is an increasing awareness of novel techniques that do not require labelling of the ligand or the receptor, and that allow virtually any complex to be screened with minimal assay development. This review focuses on three major label-free screening platforms: surface plasmon resonance biosensors, acoustic biosensors, and calorimetric biosensors. Scientists in both academia and industry are using biosensors in areas that encompass almost all areas drug discovery, diagnostics, and the life sciences. The capabilities and advantages of each technique are compared and key applications involving small molecules, proteins, oligonucleotides, bacteriophage, viruses, bacteria, and cells are reviewed. The role of the interface between the biosensor surface (in the case of SPR and acoustic biosensors) and the chemical or biological systems to be studied is also covered with attention to the covalent and non-covalent coupling chemistries commonly employed.

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Section: Surface Chemistrymentioning

confidence: 99%

Label-free screening of bio-molecular interactions

Cooper

2003

Analytical and Bioanalytical Chemistry

414

308

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“…Multivalency can be conveniently described by an effective concentration (C eff ) term that represents a probability of interaction between two interlinked reactive or complementary entities and symbolizes the concentration of one of the reacting or interacting functionalities as experienced by its counterpart (4, 5). Versatile model systems to investigate multivalent noncovalent interactions at the dynamic interface between cell membranes and the surrounding aqueous solution include self-assembled monolayers (SAMs) (6-11), nanoparticles (12-14), solid-supported lipid bilayers (15, 16), and bilayer vesicles (17-19).Metal-ligand coordination has been exploited to generate complex molecular architectures with specific topology, high stability, and original properties in aqueous solution (16,20,21). The N-nitrilotriacetic acid-histidine interaction is particularly interesting in a biological context.…”

mentioning

confidence: 99%

“…Multivalency can be conveniently described by an effective concentration (C eff ) term that represents a probability of interaction between two interlinked reactive or complementary entities and symbolizes the concentration of one of the reacting or interacting functionalities as experienced by its counterpart (4,5). Versatile model systems to investigate multivalent noncovalent interactions at the dynamic interface between cell membranes and the surrounding aqueous solution include self-assembled monolayers (SAMs) (6)(7)(8)(9)(10)(11), nanoparticles (12)(13)(14), solid-supported lipid bilayers (15,16), and bilayer vesicles (17)(18)(19).…”

mentioning

confidence: 99%

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Intravesicular and intervesicular interaction by orthogonal multivalent host–guest and metal–ligand complexation

Lim

Crespo-Biel

Stuart

et al. 2007

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

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Host vesicles composed of amphiphilic ␤-cyclodextrin CD1 recognize metal-coordination complexes of the adamantyl-functionalized ethylenediamine ligand L via hydrophobic inclusion in the ␤-cyclodextrin cavities at the vesicle surface. In the case of Cu(II) and L, the resulting coordination complex was exclusively CuL2, and the interaction with the host vesicles was intravesicular, unless the concentration of metal complex and vesicles was high (>0.1 mM). In the case of Ni(II) and L, a mixture was formed consisting of mainly NiL and NiL2, the interaction with the host vesicles was effectively intervesicular, and addition of the guest-metal complex resulted in aggregation of the vesicles into dense, multilamellar clusters even in dilute solution [1 M Ni(II)]. The metal-L complex could be eliminated by a strong chelator such as EDTA, and the intervesicular interaction could be suppressed by a competitor such as unmodified ␤-cyclodextrin. The result from this investigation is that the strongest metal-coordination complex [Cu(II) with L] binds exclusively intravesicularly, whereas the weakest metal-coordination complex [Ni(II) with L] binds predominantly intervesicularly and is the strongest interfacial binder. These experimental observations are confirmed by a thermodynamic model that describes multivalent orthogonal interactions at interfaces.self-assembly ͉ vesicles ͉ cyclodextrins M ultivalent, noncovalent interactions at the interface of cell membranes are involved in a variety of biological processes such as cell-cell signaling, pathogen identification, and inflammatory response (1). Multivalent binding events have collective properties that are qualitatively and quantitatively different from the contributing monovalent interactions. For example, multivalent interactions lead to higher binding affinities and can afford larger contact areas between surfaces (1-3). Multivalency can be conveniently described by an effective concentration (C eff ) term that represents a probability of interaction between two interlinked reactive or complementary entities and symbolizes the concentration of one of the reacting or interacting functionalities as experienced by its counterpart (4, 5). Versatile model systems to investigate multivalent noncovalent interactions at the dynamic interface between cell membranes and the surrounding aqueous solution include self-assembled monolayers (SAMs) (6-11), nanoparticles (12-14), solid-supported lipid bilayers (15, 16), and bilayer vesicles (17-19).Metal-ligand coordination has been exploited to generate complex molecular architectures with specific topology, high stability, and original properties in aqueous solution (16,20,21). The N-nitrilotriacetic acid-histidine interaction is particularly interesting in a biological context. N-nitrilotriacetic acidfunctionalized lipids (22, 23) and SAMs (24, 25) have been used to immobilize proteins through multivalent interactions. In a comparable approach, the multivalent binding of Cu(II) ions to a membrane-bound dansyl-ethylenediamine conjugat...

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“…The use of metal ion coordination to target the adsorption of proteins to lipid membranes has received much attention previously. 1,[7][8][9][10][11][12][13][14][15][16][17][18][19] Mixtures of metal-chelating lipids with other lipids are being investigated for protein detection schemes, as protein adsorption can lead to in-plane rearrangements of the lipids detectable by fluorescence techniques. 12,13 The present study explored adsorbed peptide structures involving the α-helix motif.…”

Section: Introductionmentioning

confidence: 99%

Synthetic Polypeptide Adsorption to Cu-IDA Containing Lipid Films: A Model for Protein−Membrane Interactions

Kent¹,

Yim²,

Murton³

et al. 2008

Langmuir

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Adsorption of synthetic alanine-rich peptides to lipid monolayers was studied by X-ray and neutron reflectivity, grazing incidence X-ray diffraction (GIXD), and circular dichroic spectroscopy. The peptides contained histidine residues to drive adsorption to Langmuir monolayers of lipids with iminodiacetate headgroups loaded with Cu 2+ . Adsorption was found to be irreversible with respect to bulk peptide concentration. The peptides were partially helical in solution at room temperature, the temperature of the adsorption assays. Comparisons of the rate of binding and the structure of the adsorbed layer were made as a function of the number of histidines (from 0 to 2) and also as a function of the positioning of the histidines along the backbone. For peptides containing two histidines on the same side of the helical backbone, large differences were observed in the structure of the adsorbed layer as a function of the spacing of the histidines. With a spacing of 6 Å, there was a substantial increase in helicity upon binding (from 17% to 31%), and the peptides adsorbed to a final density approaching that of a nearly completed monolayer of α-helices adsorbed side-on. The thickness of the adsorbed layer (17 ± 2.5 Å) was slightly greater than the diameter of α-helices, suggesting that the free, unstructured ends extended into solution. With a spacing of 30 Å between histidines, a far weaker increase in helicity upon binding was observed (from 13% to 19%) and a much lower packing Correspondence to: M. S. Kent. Supporting Information Available: Additional figures as described in the text. This material is available free of charge via the Internet at http://pubs.acs.org. NIH Public Access Author ManuscriptLangmuir. Author manuscript; available in PMC 2010 July 5. NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript density resulted. The thickness of the adsorbed layer (10 ± 4 Å) was smaller, consistent with the ends being bound to the monolayer. Striking differences were observed in the interaction of the two types of peptide with the lipid membrane by GIXD, consistent with binding by two correlated sites only for the case of 6 Å spacing. All these results are attributed to differences in spatial correlation between the histidines as a function of separation distance along the backbone for these partially helical peptides. Finally, control over orientation was demonstrated by placing a histidine on an end of the sequence, which resulted in adsorbed peptides oriented perpendicular to the membrane.

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Design of Supported Membranes Tethered via Metal-Affinity Ligand-Receptor Pairs

Cited by 45 publications

References 41 publications

Label-free screening of bio-molecular interactions

Label-free screening of bio-molecular interactions

Intravesicular and intervesicular interaction by orthogonal multivalent host–guest and metal–ligand complexation

Synthetic Polypeptide Adsorption to Cu-IDA Containing Lipid Films: A Model for Protein−Membrane Interactions

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