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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2006

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Glutamine-binding protein from Escherichia coli specifically binds a wheat gliadin peptide allowing the design of a new porous silicon-based optical biosensor.

Anno di pubblicazione: 2006

Formato: Elettronico Cartaceo

Autori: De Stefano L, Rossi M, Staiano M, Mamone G, Parracino A, Rotiroti L, Rendina I, Rossi M, D'Auria S.

Affiliazioni autori: IBP-CNR Istituto di Scienze dell'Alimentazione CNR, Avellino

Autori CNR:

  • GIANFRANCO MAMONE
  • MAURO ROSSI

Lingua: inglese

Abstract: In this work, the binding of the recombinant glutamine-binding protein (GlnBP) from Escherichia coli to gliadin peptides, toxic for celiac patients, was investigated by mass spectrometry experiments and optical techniques. Mass spectrometry experiments demonstrated that GlnBP binds the following amino acid sequence: XXQPQPQQQQQQQQQQQQL, present only into the toxic prolamines. The binding of GlnBP to gliadin suggested us to design a new optical biosensor based on nanostructured porous silicon (PSi) for the detection of trace amounts of gliadin in food. The GlnBP, which acts as a molecular probe for the gliadin, was covalently linked to the surface of the PSi wafer by a proper passivation process. The GlnBP-gliadin interaction was revealed as a shift in wavelength of the fringes in the reflectivity spectrum of the PSi layer. The GlnBP, covalently bonded to the PSi chip, selectively recognized the toxic peptide. Finally, the sensor response to the protein concentration was measured in the range 2.0-40.0 microg/L and the sensitivity of the sensor was determined.

Pagine da: 1241

Pagine a: 1245

Rivista:

Journal of proteome research American Chemical Society,
Paese di pubblicazione: Stati Uniti d'America
Lingua: inglese
ISSN: 1535-3893

Numero volume: 5

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