title: In vitro digestive stability of complexes between gliadin and synthetic blocking peptides.
abstract: 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.
authors.affiliation: Department of Chemical and Biological Engineering/Food Science, Chalmers University of Technology, Gothenburg, Sweden. karolina.hoffmann@chalmers.se
authors.forename: Karolina
authors.initials: K
authors.lastname: Hoffmann
authors.forename: Nils-Gunnar
authors.initials: NG
authors.lastname: Carlsson
authors.forename: Marie
authors.initials: M
authors.lastname: Alminger
authors.forename: Tingsu
authors.initials: T
authors.lastname: Chen
authors.forename: Agnes
authors.initials: A
authors.lastname: Wold
authors.forename: Olof
authors.initials: O
authors.lastname: Olsson
authors.forename: Ann-Sofie
authors.initials: AS
authors.lastname: Sandberg
mesh_terms: D000818:Animals; D000915:Antibody Affinity / Q000187:drug effects / Q000276:immunology; D000937:Antigen-Antibody Reactions / Q000187:drug effects / Q000276:immunology; D001666:Binding Sites, Antibody / Q000187:drug effects / Q000276:immunology; D001709:Biotechnology; D015153:Blotting, Western; D002851:Chromatography, High Pressure Liquid; D004064:Digestive System / Q000201:enzymology* / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000187:drug effects / Q000276:immunology; D005903:Gliadin / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D007070:Immunoglobulin A / Q000276:immunology; D007074:Immunoglobulin G / Q000276:immunology; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D013552:Swine
chemical_list: D000939:Epitopes; D007070:Immunoglobulin A; D007074:Immunoglobulin G; D010455:Peptides; D005903:Gliadin