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Structural Analysis and Caco-2 Cell Permeability of the Celiac-Toxic A-Gliadin Peptide 31-55 (Articolo in rivista)
- Type
- Label
- Structural Analysis and Caco-2 Cell Permeability of the Celiac-Toxic A-Gliadin Peptide 31-55 (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/jf3045523 (literal)
- Alternative label
Iacomino G., Fierro O., D'Auria S., Picariello G., Ferranti P.,
Liguori C., Addeo F., and Mamone G. (2013)
Structural Analysis and Caco-2 Cell Permeability of the Celiac-Toxic A-Gliadin Peptide 31-55
in Journal of agricultural and food chemistry; ACS, American chemical society, Washington, DC (Stati Uniti d'America)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Iacomino G., Fierro O., D'Auria S., Picariello G., Ferranti P.,
Liguori C., Addeo F., and Mamone G. (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Titolo
- Structural Analysis and Caco-2 Cell Permeability of the Celiac-Toxic A-Gliadin Peptide 31-55 (literal)
- 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. (literal)
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