Abstract
BackgroundThe interaction between biotin and avidin is utilized in a wide range of assay and diagnostic systems. A robust material capable of binding biotin should offer scope in the development of reusable assay materials and biosensor recognition elements.ResultsBiotin-selective thin (3–5 nm) films have been fabricated on hexadecanethiol self assembled monolayer (SAM) coated Au/quartz resonators. The films were prepared based upon a molecular imprinting strategy where N,N'-methylenebisacrylamide and 2-acrylamido-2-methylpropanesulfonic acid were copolymerized and grafted to the SAM-coated surface in the presence of biotin methyl ester using photoinitiation with physisorbed benzophenone. The biotinyl moiety selectivity of the resonators efficiently differentiated biotinylated peptidic or carbohydrate structures from their native counterparts.ConclusionsMolecularly imprinted ultra thin films can be used for the selective recognition of biotinylated structures in a quartz crystal microbalance sensing platform. These films are stable for periods of at least a month. This strategy should prove of interest for use in other sensing and assay systems.
Highlights
The interaction between biotin and avidin is utilized in a wide range of assay and diagnostic systems
This interaction has been exploited as an integral component in many biochemical assays and diagnostics [3,4], examples include methods based upon spectrophotometry [5], HPLC [6], radioligand binding [7], electroanalysis [8] and bioassays, e.g. ELISA [9]
atomic force microscopy (AFM) studies of the topographical features of the surfaces, Figure 3a-c, revealed that the self assembled monolayer (SAM)-Au/quartz surfaces were uniformly coated with molecularly imprinted polymer (MIP) and REF films
Summary
The interaction between biotin and avidin is utilized in a wide range of assay and diagnostic systems. In humans and other mammals, it serves as a transient carrier of the carboxylate group and is involved in gluconeogenesis as well as fatty acid biosynthesis [2]. It is significant on account of its stable and strong interaction (Kd of ~10−15 mol/L) with the proteins avidin and streptavidin. This interaction has been exploited as an integral component in many biochemical assays and diagnostics [3,4], examples include methods based upon spectrophotometry [5], HPLC [6], radioligand binding [7], electroanalysis [8] and bioassays, e.g. ELISA [9]. Synthetic polymers capable of binding biotin could provide an interesting alternative as they are reusable
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