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GRENOBLE,France—High-throughput technologies like microarrays have proven a boon to genomic studies, but their parallels in the protein world have come more slowly. Most of the metabolic action of a cell occurs at the protein level, however, so efforts to improve the status quo have been rampant. With this in mind, researchers at the Institut National de la Santé et de la Recherche Médicale have combined two analytical techniques to create a system that can monitor protein-peptide interactions in real time. They presented their efforts in Clinical Chemistry (2006, 52, 255-262).

 

The researchers immobilized peptides onto discrete locations on a gold wafer, much as others have spotted DNA microarrays. They then used a form of surface plasmon resonance (SPR) called SPR imaging to perform parallel analysis of multiple binding events on a single chip.

 

They tested their chip system with a variety of peptides and immune sera and found the system offered high specificity and good regeneration characteristics. Furthermore, using serial dilutions, they found they could detect very small interactions in complex media, and in a manner at least as sensitive as ELISAs. The researchers are confident that by allowing clinicians to identify specific antibodies early, they can facilitate earlier prognosis of disease and therapy optimization.

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