Celiac disease is a chronic autoimmune disease that begins in response to gluten intake. /freepik
A study led by scientists from the Barcelona Institute of Molecular Biology (IBMB-CSIC) has identified a molecule that can counteract the effects of toxic peptides. celiac diseaseA chronic autoimmune disease that begins in response to gluten ingestion.
it’s about do not askfound naturally in the digestive fluid of carnivorous plants Nepenthes Ventrata, The authors decipher the mechanism of action, structure and most relevant features of the molecule with a view to potential treatment of the pathology. The study has been published in nature communication,
an inflammatory reaction in the intestine
Celiac disease is triggered by various prolamin-rich proteins found in grains. When they are digested in the stomach, they break down into smaller pieces (Peptides) which can be toxic. Among these peptides, the most relevant is the 33-mer, which is a fragment of alpha-gliadin, a wheat glycoprotein.
33-mer is able to resist gastric acid from the stomach, reaches the small intestine and, once there, crosses the intestinal mucosa. In the case of people with celiac disease, this peptide is particularly readily available in a . gets tied to immune system receptor (human leukocyte antigen or HLA), which triggers an autoimmune and inflammatory response that gives rise to a whole range of disease-specific manifestations.
The results suggest that naproxen can degrade the 33-mer peptide before it reaches the intestine, which may inhibit Autoimmune inflammatory response.
Role of Naprosyn
scientists have obtained Recombinant Human Cell Culture To obtain enough naproxen. They have identified and determined its mechanism of action, as well as its ability to destroy gliadin and the 33-mer peptide. experiments in vivo Show in mouse model that molecule is effective degrading both structures in the stomach.
They have also solved the three-dimensional structure and chemical mechanism of action of naproxen and established characteristics such as its thermal stability, its pH profile, and its latency period.
These factors are very important for the potential development of prevention or treatment, which did not exist until now. One promising avenue is molecules that destroy toxic peptides, and that can be administered orally, similar to lactase pills taken by lactose intolerant people, the study authors explain.
future therapeutic applications
Such a treatment must have a molecule capable of breaking down toxic peptides and be harmful to the gutThe researchers say it must be efficient enough to break down toxic peptides in appropriate amounts, and be active before they pass into the gut.
“We have been able to verify that naproxen has great potential as a drug, as it is much more active in extreme conditions of stomach digestion than other candidate proteolytic enzymes currently under study for therapeutic application. ,” they tell. F Xavier Gomis-Ruth,
“We are now going to have more specific tests to verify this capability before moving on to clinical trials and working with mutant molecules that may be even more efficient.”
for its part, Francisco Jose Perez CanoA researcher at the University of Barcelona and other authors commented that “the 33-mer is the most toxic peptide of humans originating from gliadin and it remains to be seen whether its elimination will be sufficient to eliminate the pathophysiological manifestations and reactions of celiac disease.” “.