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Fabio Cimaglia, Giovanni Potente, Maurizio Chiesa, Giovanni Mita and Gianluca Bleve
Celiac disease is an immune-mediated enteropathy precipitated by the ingestion of gluten-containing foods in genetically predisposed children and adults. After a positive diagnosis for celiac disease, the only available treatment is to adopt a gluten-free diet, and evaluation of the absence of gluten in foods is crucial for the health of celiac patients. In the present study, a recombinant glutamine-binding protein (GlnBP) from Escherichia coli showed its ability to recognize peptides deriving from digested wheat flour. GlnBP and the commercially available 4F3 monoclonal antibody, raised against a region of the α-gliadin peptide 33-mer from wheat, demonstrated the ability to detect gliadin extracted from wheat flour. Recombinant GlnBP and 4F3 monoclonal antibody were used as new capture agents for the development of a protein chip able to detect gluten in foods. The protein microarray system has proven to detect the presence of gliadin in a range of concentrations between 500 and 5 ppm.