Continuous-flow synthesis of alpha-gliadin peptides in an ultrasonic field and assay of their inhibition of intestinal sucrase activity
Language English Country United States Media print
Document type Journal Article
PubMed
1839365
Knihovny.cz E-resources
- MeSH
- Adenovirus Early Proteins MeSH
- Duodenum drug effects enzymology MeSH
- Endorphins chemistry MeSH
- Gliadin chemical synthesis chemistry pharmacology MeSH
- Protein Conformation MeSH
- Chick Embryo MeSH
- Molecular Sequence Data MeSH
- Oncogene Proteins, Viral chemistry MeSH
- Peptide Fragments chemical synthesis chemistry pharmacology MeSH
- Sucrase antagonists & inhibitors MeSH
- Amino Acid Sequence MeSH
- In Vitro Techniques MeSH
- Ultrasonics MeSH
- Animals MeSH
- Check Tag
- Chick Embryo MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Adenovirus Early Proteins MeSH
- beta-casomorphins MeSH Browser
- Endorphins MeSH
- Gliadin MeSH
- Oncogene Proteins, Viral MeSH
- Peptide Fragments MeSH
- Sucrase MeSH
Three dodecapeptide amides derived from the amino acid sequence of alpha-gliadin and four of their analogues were synthesized by continuous-flow solid-phase multiple peptide synthesis. Ultrasonic field conditions accelerated the coupling reaction without affecting purity. Biological tests of the synthetic fragments showed the relevance of toxicity prediction for preselection of immunogenic alpha-gliadin fragments.
Binding of gliadin to lymphoblastoid, myeloid and epithelial cell lines
