Specific recognition and formation of two- dimensional streptavidin domains in monolayers: applications to molecular devices

Ahlers, Michael; Blankenburg, R.; Grainger, David W.; Meller, P.; Ringsdorf, Helmut; Salesse, Christian

doi:10.1016/0040-6090(89)90059-x

Cited by 84 publications

(43 citation statements)

References 10 publications

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“…(1), describes the effective intermolecular attractions between proteins. The reason for including protein-protein attractions is that there is experimental evidence that streptavidin on lipid layers tends to form two dimensional crystals 40–43

\frac{β U_{italicinter}}{A} = \frac{β χ}{2 υ_{w}} \int normald z σ_{b} true \sum_{α_{1}} P_{b} false(α_{1} false) υ_{pro} false(α_{1}; z false) < ϕ_{pro} false(z false) >

where the χ parameter is a measure of the strength of the attractions between the proteins.…”

Section: Molecular Theoretical Approachmentioning

confidence: 99%

Streptavidin−Biotin Binding in the Presence of a Polymer Spacer. A Theoretical Description

Ren

Carvajal²,

Shull³

et al. 2009

Langmuir

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The binding of streptavidin to biotin located at the terminal ends of poly(ethylene oxide) tethered to a planar surface is studied using molecular theory. The theoretical model is applied to mimic experiments (Langmuir 2008(Langmuir , 24, 2472 performed using drop-shape analysis to study receptorligand binding at the oil/water interface. Our theoretical predictions show very good agreements with the experimental results. Furthermore, the theory enables us to study the thermodynamic and structural behavior of the PEO-biotin+streptavidin layer. The interfacial structure, shown by the volume fraction profiles of bound proteins and polymers, indicates that the proteins form a thick layer supported by stretched polymers, where the distribution of bound proteins is greater than the thickness of the height of one layer of proteins. When the polymer spacer is composed of PEO (3000), a thick layer with multi-layers of proteins is formed, supported by the stretched polymer chains. It was found that thick multi-layers of proteins are formed when long spacers are present or at very high protein surface coverages on short spacers. This shows that the flexibility of the polymer spacer plays an important role in determining the structure of the bound proteins due to their ability to accommodate highly distorted conformations to optimize binding and protein interactions. Protein domains are predicted when the amount of bound proteins is small due to the existence of streptavidinstreptavidin attractive interactions. As the number of proteins is increased, the competition between attractive interactions and steric repulsions determines the stability and structure of the bound layer. The theory predicts that the competition between these two forces leads to a phase separation at higher protein concentrations. The point where this transition happens depends on both spacer length and protein surface coverage and is an important consideration for practical applications of these and other similar systems. If the goal is to maximize protein binding, it is favorable to be above the layer transition, as multiple layers can accommodate greater bound protein densities. On the other hand, if the goal is to use these bound proteins as a linker group to build more complex structures, such as when avidin or streptavidin serves as a linker between two biotinylated polymers or proteins, the optimum is to be below the layer transition such that all bound linker proteins are available for further binding. II. INTRODUCTIONLigand-receptor interactions are an important control mechanism in many biological systems. For example, the binding of extracellular matrix proteins to specific receptors on the cell surface triggers signal transduction pathways allowing the cell to sense and react to its environment in Correspondence to: Igal Szleifer. NIH Public Access Author ManuscriptLangmuir. Author manuscript; available in PMC 2010 October 20. NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscriptways such as aggregating with ot...

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\frac{β U_{italicinter}}{A} = \frac{β χ}{2 υ_{w}} \int normald z σ_{b} true \sum_{α_{1}} P_{b} false(α_{1} false) υ_{pro} false(α_{1}; z false) < ϕ_{pro} false(z false) >

where the χ parameter is a measure of the strength of the attractions between the proteins.…”

Section: Molecular Theoretical Approachmentioning

confidence: 99%

Streptavidin−Biotin Binding in the Presence of a Polymer Spacer. A Theoretical Description

Ren

Carvajal²,

Shull³

et al. 2009

Langmuir

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“…The very high specific binding affinity (K a ∼ 10 13 -10 15 M −1 ) [11] between streptavidin and its ligand biotin makes this system a very attractive model for studying surface recognition processes. Previous studies using biotinylated lipids at the air-liquid and solid-liquid interfaces have demonstrated the specific and rapid binding of streptavidin to biotin [12][13][14][15][16][17][18]. Streptavidin has a well-known ability to assemble into optically anisotropic two-dimensional (2D) crystals at these interfaces [18][19][20][21] The prerequisite for the 2D protein crystallization is the mobility (lateral diffusion) of proteins at the interface.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of streptavidin onto biotin-functionalized Langmuir–Schaefer binary monolayers chemisorbed on gold

Ihalainen

Peltonen

2004

Sensors and Actuators B: Chemical

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“…protein tectonics) remains challenging. [21][22][23][24][30][31][32][33][34] In the spirit of coordination polymers, we reasoned that one may exploit the versatility of transition-metal connectors in conjunction with proteins bearing tethered ligands to create discrete one-, two-, or three-dimensional metalorganic protein frameworks (MOPF; Figure 1). For this proof-of-principle study, we used a linear Fe(terpy) 2 moiety (terpy = terpyridine) bearing four biotin anchors, [Fe(Biot 2 -terpy) 2 ] 2+ complex (the connector), in conjunction with streptavidin (hereafter referred to as Sav, the linker) to afford a one-dimensional MOPF.…”

mentioning

confidence: 99%

Hierarchical Self‐Assembly of One‐Dimensional Streptavidin Bundles as a Collagen Mimetic for the Biomineralization of Calcite

et al. 2007

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Specific recognition and formation of two- dimensional streptavidin domains in monolayers: applications to molecular devices

Cited by 84 publications

References 10 publications

Streptavidin−Biotin Binding in the Presence of a Polymer Spacer. A Theoretical Description

Streptavidin−Biotin Binding in the Presence of a Polymer Spacer. A Theoretical Description

Immobilization of streptavidin onto biotin-functionalized Langmuir–Schaefer binary monolayers chemisorbed on gold

Hierarchical Self‐Assembly of One‐Dimensional Streptavidin Bundles as a Collagen Mimetic for the Biomineralization of Calcite

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