Oriented Binding of the His6-Tagged Carboxyl-Tail of the L-type Ca2+ Channel α1-Subunit to a New NTA-Functionalized Self-Assembled Monolayer

Gamsjaeger, Roland; Wimmer, Barbara; Kahr, Heike; Tinazli, Ali; Pićurić, Srdjan; Lata, Suman; Tampé, Robert; Maulet, Yves; Gruber, Hermann J.; Hinterdorfer, Peter; Romanin, Christoph

doi:10.1021/la0498206

Cited by 33 publications

(21 citation statements)

References 57 publications

(93 reference statements)

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“…Using ligands which bind to a defined region of the adsorbed protein, force-displacement curves are acquired, and the quantity of formed complexes gives an estimate of the amount of protein oriented in such a way as to allow ligand binding. (See also [1117,1141]. ) Gutsmann et al [1142] have used short cantilevers (length smaller than 20 mm) to improve the force resolution below 10 pN range.…”

Section: Rupture Force Of Specific Interactionsmentioning

confidence: 99%

Force measurements with the atomic force microscope: Technique, interpretation and applications

Butt

Cappella

Kappl

2005

Surface Science Reports

3,198

2,949

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Section: Rupture Force Of Specific Interactionsmentioning

confidence: 99%

Force measurements with the atomic force microscope: Technique, interpretation and applications

Butt

Cappella

Kappl

2005

Surface Science Reports

3,198

2,949

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“…Specific interactions between glutathione and glutathione S-transferase (GST) or between Ni-NTA (nickel-nitrilotriacetic acid) and (His) 6 have been used to attach GST-/(His) 6 -tagged proteins to the AFM cantilever. Methods to covalently bind glutathione or Ni-NTA to an AFM cantilever via a polyethylene glycol (PEG) linker and to attach GST or (His) 6 -fused protein to this cantilever have been developed [41,42] (Fig. 2).…”

Section: Piconewton Scale Force Measurementmentioning

confidence: 99%

“…The instrumentation and application of AFM have been enormously fruitful due to the development of sharp cantilevers for molecular imaging [36][37][38], cantilever modification techniques for single-molecule force measurement [39][40][41][42][43], and fast-scanning devices for realtime imaging [44][45][46][47][48].…”

mentioning

confidence: 99%

Nuclear architecture and chromatin dynamics revealed by atomic force microscopy in combination with biochemistry and cell biology

Hirano

Takahashi

Kumeta

et al. 2008

Pflugers Arch - Eur J Physiol

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The recent technical development of atomic force microscopy (AFM) has made nano-biology of the nucleus an attractive and promising field. In this paper, we will review our current understanding of nuclear architecture and dynamics from the structural point of view. Especially, special emphases will be given to: (1) How to approach the nuclear architectures by means of new techniques using AFM, (2) the importance of the physical property of DNA in the construction of the higher-order structures, (3) the significance and implication of the linker and core histones and the nuclear matrix/scaffold proteins for the chromatin dynamics, (4) the nuclear proteins that contribute to the formation of the inner nuclear architecture. Spatio-temporal analyses using AFM, in combination with biochemical and cell biological approaches, will play important roles in the nano-biology of the nucleus, as most of nuclear structures and events occur in nanometer, piconewton and millisecond order. The new applications of AFM, such as recognition imaging, fast-scanning imaging, and a variety of modified cantilevers, are expected to be powerful techniques to reveal the nanostructure of the nucleus.

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“…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 conjugate (26) and of Zn(II) to a membrane-embedded dipicolylamine receptor (27) has been reported.…”

mentioning

confidence: 99%

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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Oriented Binding of the His₆-Tagged Carboxyl-Tail of the L-type Ca²⁺ Channel α₁-Subunit to a New NTA-Functionalized Self-Assembled Monolayer

Cited by 33 publications

References 57 publications

Force measurements with the atomic force microscope: Technique, interpretation and applications

Force measurements with the atomic force microscope: Technique, interpretation and applications

Nuclear architecture and chromatin dynamics revealed by atomic force microscopy in combination with biochemistry and cell biology

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

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