A SMALL PEPTIDE FROM DURUM-WHEAT GLIADIN PREVENTS CELL AGGLUTINATION INDUCED BY PROLAMIN-PEPTIDES TOXIC IN CELIAC-DISEASE

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. A n amino acid sequence was identified in the 1157.5 Da peptide as being related to the largest common sequences previously detected in a seri es of bread wheat toxic peptides by other authors. (C) 1997 Elsevier S cience Ireland Ltd.