Molecular recognition processes at functionalized lipid surfaces: a neutron reflectivity study

Lösche, Mathias; Piepenstock, M.; Vaknin, David; Als‐Nielsen, J.

doi:10.1016/0040-6090(92)90367-k

Cited by 6 publications

(1 citation statement)

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“…Self-assembled monolayers of proteins formed at lipid monolayers and liposome surfaces have been studied using biotin−avidin or suger-lectin interaction . The specific interaction − of streptavidin (SA) with biotin-attached lipids spread at the air−water interface − leads to a formation of optically anisotropic two-dimensional (2-D) streptavidin crystals, where two of the original four biotin-binding sites remain free. − The SA layer docked on the biotinylated lipid monolayer can thus act as a template to immobilize other functionalized biotin molecules, − or bis-biotin couplers can be used to bridge two SA layers …”

Section: Introductionmentioning

confidence: 99%

Protein−DNA Double and Triple Layers: Interaction of Biotinylated DNA Fragments with Solid Supported Streptavidin Layers

Ijiro¹,

Ringsdorf²,

Birch-Hirschfeld³

et al. 1998

Langmuir

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The specific interaction of streptavidin with biotinylated lipids at the air-water interface leads to a formation of optically anisotropic two-dimensional streptavidin (2-D) crystals, where two of the original four biotin-binding sites remain free. These assembled streptavidin matrixes were used as a template for docking of double-stranded oligonucleotides biotinylated at a terminal or a centered position. A biotinylated lipid monolayer was deposited on an electrode of a quartz crystal microbalance (QCM), and docking processes of the protein and the oligonucleotides were detected as frequency changes related by mass changes on the QCM. The bis-biotinylated double-stranded oligonucleotides bound to the primary streptavidin layers made it possible to engineer protein-DNA-protein triple layers. Hydrolysis by a restriction endonuclease indicates that the biotinylated DNA bound to the streptavidin layers remains bioactive.

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