Blocking peptides decrease tissue transglutaminase processing of gliadin in vitro
Journal article, 2009

Tissue transglutaminase (tTG) plays an important role in celiac disease pathology as it catalyzes deamidation and cross-linking of specific gluten peptides and converts them into potent epitopes recognized by intestinal T-cells. We investigated whether synthetic peptides with high affinity to gliadin could alter tTG activity on gliadin and whole gluten digest. The immobilized substrates were incubated with synthetic peptides identified by the phage display technique and a control peptide with no affinity to gliadin. Transglutaminase activity was measured with time resolved fluorescence. The mean tTG activity, compared to that of the control without the peptides, was reduced by 31, 33, and 36% for three selected gliadin-binding peptides, and 30% for the peptide pool (P <= 0.001-0.004) when gliadin was the substrate. Finally, substrate specificity experiments suggested that avenin was processed in a manner similar that used for gliadin during in vitro assays with tTG. The results showed that the blocking peptides efficiently reduced tTG processing of gliadin in vitro, and this strategy will be further investigated as an alternative therapy for celiac disease.


synthetic peptides

tissue transglutaminase

celiac disease

time resolved fluoroscence


Karolina Hoffmann

Chalmers, Chemical and Biological Engineering, Life Sciences

Marie Alminger

Chalmers, Chemical and Biological Engineering, Life Sciences

Thomas Andlid

Chalmers, Chemical and Biological Engineering, Life Sciences

Tingsu Chen

University of Gothenburg

Academic Health Center

Olof Olsson

University of Gothenburg

Ann-Sofie Sandberg

Chalmers, Chemical and Biological Engineering, Life Sciences

Journal of Agricultural and Food Chemistry

0021-8561 (ISSN) 1520-5118 (eISSN)

Vol. 57 21 10150-10155

Subject Categories

Biological Sciences

Immunology in the medical area

Areas of Advance

Life Science Engineering (2010-2018)



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