A small peptide from durum wheat gliadin prevents cell agglutination induced by prolamin-peptides toxic in coeliac disease

Toxicology. 1997 Jul 11;120(3):207-13. doi: 10.1016/s0300-483x(97)00060-7.

Abstract

A peptide (m.w. 1157.5 Da) able to prevent the agglutination of K562(S) cells induced by the peptic-tryptic prolamine digests of the cereals toxic in coeliac disease (i.e. bread wheat, rye, barley and oat) was characterized as one of the components of the peptic-tryptic digest of durum wheat gliadin. This peptide was synthesized in a high degree of purity with the solid phase method with the Applied Biosystem 431A. An amino acid sequence was identified in the 1157.5 Da peptide as being related to the largest common sequences previously detected in a series of bread wheat toxic peptides by other authors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agglutination / drug effects*
  • Celiac Disease / chemically induced*
  • Celiac Disease / prevention & control
  • Cell Adhesion / drug effects
  • Chromatography, Affinity
  • Gliadin / chemistry*
  • Humans
  • Leukemia, Myeloid / drug therapy*
  • Leukemia, Myeloid / pathology
  • Molecular Sequence Data
  • Oligopeptides / chemical synthesis
  • Oligopeptides / isolation & purification
  • Oligopeptides / pharmacology*
  • Plant Proteins / toxicity
  • Prolamins
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Triticum
  • Tumor Cells, Cultured / pathology

Substances

  • Oligopeptides
  • Plant Proteins
  • Prolamins
  • Gliadin