Surface plasmon resonance biotin

Immunosensors have been developed commercially mostly for medical purposes but would appear to have considerable potential for food analysis. The Pharmacia company has developed an optical biosensor, which is a fully automated continuous-flow system which exploits the phenomenon of surface plasmon resonance (SPR) to detect and measure biomolecular interactions. The technique has been validated for determination of folic acid and biotin in fortified foods (Indyk, 2000 Bostrom and Lindeberg, 2000), and more recently for vitamin Bi2. This type of technique has great potential for application to a wide range of food additives but its advance will be linked to the availability of specific antibodies or other receptors for the various additives. It should be possible to analyse a whole range of additives by multi-channel continuous flow systems with further miniaturisation. 

AB, Switzerland) in SPR (surface plasmon resonance) studies. The PLL-PEG-biotin-sAV was used for microarray studies as described for the commercial product. A detailed description of the design and physical and chemical characterization of the PLL-grafted PEG monolayer is provided by Ruiz-Taylor et al. (2001). 

The avidin-biotin interaction has also been used to immobilize antibodies and proteins, especially in commercial systems based on surface plasmon resonance (SPR) measurements (e.g., the BIAcore). The extraordinary affinity (Kl 10-15 M) of avidin (or its bacterial relative, streptavidin) for the vitamin biotin is the basis of this immobilization procedure. A solid support (e.g., glass beads, sensor chip, optical fiber) covered with avidin can be used as an activated carrier for a very sturdy immobilization of previously biotinylated antibodies. In spite of the many methods for biotinylating proteins described in the literature, the use of biotinyl N-hydroxysuccinimide ester (BNHS) and similar derivatives, remains the most useful [65]. 

Once chemoenzymatically produced, these unnatural sialosides have demonstrated utility in a variety of biological applications. A sialoside consisting of 9-0-acetylated sialyl Tn antigen (sTn) was produced by one-pot synthesis and conjugated to human serum albumin to be used to evaluate the role of acetylation in carbohydrate-protein interactions. Para-nitrophenol-tagged sialosides can be used in a colorimetric assay to evaluate sialidase specificity. Biotin-tagged sialosides have been immobilized on a streptavidin-coated surface to study protein-carbohydrate interactions with surface plasmon resonance techniques. Size-defined... 

PEG-methacrylate was selected as the monomer to ensure biocompatibility, as PEGylated surfaces are known to inhibit protein binding. To demonstrate the accessibility of the surface azide groups, an azido-derivative of biotin was clicked to the polymer-brush-modified surface subsequently, surface plasmon resonance (SPR) was used to confirm the selective binding with streptavidin in preference to other proteins. 

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