ReviewAlimentary pharmacology & therapeutics2025
Review Article: Novel Enzyme Therapy Design for Gluten Peptide Digestion Through Exopeptidase Supplementation.
Review in Alimentary pharmacology & therapeutics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed.
- Therapeutic peptides and proteins: Status and developments in drug delivery.Journal of controlled release : official journal of the Controlled Release Society · 2026Review
- Targeted enzymatic therapy for coeliac disease.EMBO molecular medicine · 2026Article
- The Adaptable Binding Cleft of RmuAP1, a Pepsin-like Peptidase fromBiomolecules · 2025Article
- Living Gluten-Free in Romania: A National Cross-Sectional Study of Dietary Adherence in Clinically Diagnosed and Self-Reported Cases.Nutrients · 2025Article
- Electrochemistry as a Tool for Redox-Based Bio-Information Processing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Letter: Supporting the Role of Enzyme Therapy in Management of Coeliac Disease-Authors' Reply.Alimentary pharmacology & therapeutics · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundDietary peptides are increasingly linked to inflammatory gastrointestinal diseases, exemplified by coeliac disease. Coeliac disease is caused by an acquired immune response to proline- and glutamine-rich gluten peptides, which bottleneck proteolysis and provide substrates for immune recognition. Enzyme therapies aim to eliminate gluten immunogenic peptides as an adjunct to gluten-free diet.
aimsTo investigate overlooked aspects of enzyme development given difficulties in translating preclinical efficacy into clinical benefit.
methodsWe assessed mode-of-action, target organ and drug delivery in the context of digestive physiology and motility for gluten-digesting enzymes on the market or in development until 1 December 2024.
resultsMost enzymes were gastric endopeptidases specific for proline or glutamine residues. Gastric enzymes may achieve poor enzyme-substrate exposure due to limited mixing and rapid emptying of water-soluble particles. Moreover, endopeptidases cleave proteins/peptides into shorter peptides but do not systematically cleave protein into absorbable fractions. Natural digestive physiology provides thorough mixing at the intestinal brush border, which produces exopeptidases necessary to fully digest proline-rich peptides. Despite reduced activity in patients with coeliac disease, exopeptidases remain underexplored as therapeutic agents. Given limited substrate scope and end-to-end digestion, exopeptidases are ineffective as single agents, requiring functional combinations. Furthermore, vulnerability to gastric acid requires stabilisation or formulation for rapid enteric release.
conclusionsEnzymes should be stabilised throughout the gastrointestinal tract including the small intestine. Exopeptidases perform a critical function by systematically generating absorbable fractions, warranting future investigation as therapeutic agents. Sensitive and translational biomarkers are needed to better assess enzyme efficacy in real-meal conditions.
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