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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2013

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Structural Analysis and Caco-2 Cell Permeability of the Celiac-Toxic A-Gliadin Peptide 31-55

Anno di pubblicazione: 2013

Formato: Elettronico Cartaceo

Autori: Iacomino G., Fierro O., D'Auria S., Picariello G., Ferranti P., Liguori C., Addeo F., and Mamone G.

Affiliazioni autori: Istituto di Scienze dell'Alimentazione, CNR Avellino Istituto di Biochimica delle Proteine CNR Napoli Dipartimento di Agraria, Università Federico II Napoli

Autori CNR:

  • SABATO D'AURIA
  • OLGA FIERRO
  • GIUSEPPE IACOMINO
  • GIANFRANCO MAMONE
  • GIANLUCA PICARIELLO

Lingua: inglese

Abstract: ABSTRACT: Celiac disease is a chronic enteropathy caused by the ingestion of wheat gliadin and other cereal prolamines. The synthetic peptides 31-43 (P31-43) and 31-49 (P31-49) from A-gliadin are considered to be model peptides for studying innate immunity in celiac disease. Our previous study demonstrated that P31-43 and P31-49 are encrypted within peptide 31- 55 (P31-55), which is naturally released from gastropancreatic digestion and is not susceptible to hydrolysis by brush border membrane enzymes. Here, we analyzed the permeability of P31-55 through the epithelial cell layer of confluent Caco-2 cells using high-performance liquid chromatography, mass spectrometry, and fluorescence-activated cell sorting. Twenty-three percent of the P31-55 added to the apical chamber was transported to the basolateral chamber after 4 h of incubation without being degraded by hydrolysis. Treatment of Caco-2 cells with whole gliadin digests extracted from a common wheat cultivar increased the epithelial P31-55 translocation by approximately 35%. Moreover, we observed an atypical chromatographic profile consisting of a double peak. Chromatography using different column temperatures and circular dichroism highlighted the presence of more conformational structures around the amide bond of the two adjacent prolines 38 and 39. These findings confirm that P31-55 is gastrointestinally resistant and is permeable across a Caco-2 monolayer. Moreover, we hypothesize that the various conformations of P31-55 may play a role in the activation of innate immunity.

Lingua abstract: inglese

Rivista:

Journal of agricultural and food chemistry American Chemical Society, Books and Journals Division]
Paese di pubblicazione: Stati Uniti d'America
Lingua: inglese
ISSN: 0021-8561

Numero volume: 61

Numero fascicolo: 5

DOI: 10.1021/jf3045523

Referee: Sì: Internazionale

Stato della pubblicazione: Published version

Parole chiave:

  • gliadin
  • celiac disease
  • Caco-2 cell
  • gastropancreatic digestion
  • innate immunity

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