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<i>In vitro</i> digestive stability of complexes between gliadin and synthetic blocking peptides

Artikel i vetenskaplig tidskrift
Författare Karolina Hoffmann
Nils-Gunnar Carlsson
Marie Alminger
Tingsu Chen
Agnes E Wold
Olof Olsson
Ann-Sofie Sandberg
Publicerad i Biotechnology and Applied Biochemistry
Volym 58
Nummer/häfte 3
Sidor 190-197
ISSN 0885-4513
Publiceringsår 2011
Publicerad vid Institutionen för cell- och molekylärbiologi
Institutionen för biomedicin, avdelningen för infektionssjukdomar
Sidor 190-197
Språk en
Länkar dx.doi.org/10.1002/bab.27
Ämnesord celiac disease, gliadin, blocking peptides, in vitro digestion, RP, HPLC/immunochemistry, celiac-disease, allergens, proteins, cells
Ämneskategorier Biokemi, Molekylärbiologi, Immunteknik, Immunologi inom det medicinska området

Sammanfattning

Celiac disease is caused by an inappropriate immune response to incompletely digested gluten proteins. We investigated whether synthetic peptides with high affinity to wheat gliadin could be selected with a phage display technique and whether complexes between such peptides and gliadin could sustain gastric and pancreatic digestion. Two synthetic peptides, P61 and P64, were selected because of their high affinity to immobilized gliadin. They were allowed to form complexes with gliadin, whereafter the complexes were subjected to in vitro digestion with gastric and pancreatic enzymes. The digestion products were analyzed with Western blot and RP HPLC. The results showed that both peptides formed stable complexes with intact gliadin and that complexes between gliadin and peptide P64 partly resisted gastrointestinal digestion. The two peptides reduced the binding of serum anti-gliadin IgA antibodies by 12%, and 11.5%, respectively, and the binding of anti-gliadin antibodies of the IgG isotype by 13% and 10%. Thus peptides produced by a phage display technique could interact stably with gliadin partly masking epitopes for antibody binding. A combination of peptides of this kind may be used to block gliadin-immune system interactions.

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