Exopeptidase combination enhances the degradation of isotopically labelled gluten immunogenic peptides in humans.

Celiac disease is a common autoimmune-like enteropathy caused by an aberrant response to incompletely digested dietary gluten. Gluten immunogenic peptides including the immunodominant 33-mer are thought to be resistant to proteolytic digestion by human gastrointestinal peptidases. We developed a novel enzyme therapy approach to support gluten peptide digestion using a combination of two tandem-acting exopeptidases, AMYNOPEP, that complement the intrinsic enzymatic activity of intestinal brush border enterocytes. We evaluated the effects of AMYNOPEP supplementation on 33-mer degradation AMYNOPEP achieved rapid, complete amino-to-carboxyl terminal degradation of the 33-mer AMYNOPEP achieved complete degradation of the 33-mer into single amino acids and dipeptides

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Copyright © 2024 Mourabit, Römer, Bonner, Winter, Tschollar, Tzvetkov, Weitschies, Engeli and Tschollar.

Déclaration de conflit d'intérêts

Authors SM and JT were employed by AMYRA Biotech AG. EB has a consulting agreement with AMYRA Biotech AG. SR, MT, WW, and SE have contract research agreements with AMYRA Biotech AG. WT is co-founder of and shareholder in AMYRA Biotech AG. The remaining author declares that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. The author(s) declared that they were an editorial board member of Frontiers, at the time of submission. This had no impact on the peer review process and the final decision. The authors declare that this study received funding from AMYRA Biotech AG. The funder(s) had the following involvement in the study: study design, decision to publish, and preparation of the manuscript.