Relationship between gliadin peptide structure and their effect on the fetal chick duodenum
Language English Country Germany Media print
Document type Journal Article
PubMed
2014713
DOI
10.1007/bf01202623
Knihovny.cz E-resources
- MeSH
- Celiac Disease etiology MeSH
- Duodenum drug effects embryology MeSH
- Gliadin chemistry toxicity MeSH
- Chick Embryo MeSH
- Molecular Sequence Data MeSH
- Amino Acid Sequence MeSH
- Animals MeSH
- Check Tag
- Chick Embryo MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Gliadin MeSH
The tendency to form a beta-turn in alpha-gliadin was estimated using the B-cell determinant prediction program based on the Chou and Fasman probability of beta-turn formation. Six sequences possessing a high probability of beta-turn formation were found. A statistically high agreement was found between these six sequences and three areas in alpha-gliadin with the occurrence of Pro-Ser-Gln-Gln sequence which has recently been considered responsible for toxicity in coeliac disease. By means of solid-phase synthesis seven peptides were obtained covering the above-mentioned regions. Their toxicity was tested using the fetal chick duodenum. The results support the suggestion that peptides containing the sequences Pro-Ser-Gln-Gln and Gln-Gln-Gln-Pro may be involved in the pathogenesis of coeliac disease.
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