Tuesday, August 9, 2022

CSIC identifies a molecule that could be used to treat celiac disease

A study led by scientists from Barcelona’s Institute of Molecular Biology Superior Council of Scientific Inquiry (IBMB-CSIC) has identified a molecule, naproxen, that can be used orally to treat celiac disease, in the same way as lactase tablets taken by lactose intolerant people.

Specifically, naproxen, which is naturally found in the digestive fluid of carnivorous plants. Nepenthes Ventrata‘, may counteract the effects of toxic peptides that cause this chronic autoimmune disease that begins in response to gluten intake.

As revealed by the work, published in ‘Nature Communications’Naprosyn is a “promising” treatment option for celiac disease. The authors understand the molecule’s mechanism of action, its structure, as well as its most relevant features.

Celiac disease is triggered by various prolamin-rich proteins found in grains. When these proteins are digested in the stomach, they are broken down into smaller ones (peptides) that can be toxic. between these PeptidesOne of the most relevant is the 33-mer, which is a fragment of alpha-gliadin, a prolamin (vegetable glycoprotein) from wheat.

The 33-mer peptide is able to counteract gastric acid from the stomach and reach the small intestine and once there, it crosses the intestinal mucosa. In the case of people with celiac disease, 33rd It binds with particular ease to a receptor of the immune system (human leukocyte antigen or HLA), triggering an autoimmune and inflammatory response that causes a whole range of disease-specific manifestations.

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The results show that naproxen It can degrade the 33-mer peptide before reaching the intestine, which may inhibit this inflammatory autoimmune response.

Scientists have developed to obtain recombinant cultures of human cells Naprosyn in sufficient quantity. They have identified and determined the mechanism of action of naproxen, as well as its ability to destroy gliadin and the 33-mer peptide.

‘In vivo’ experiments in a murine model show that the molecule is effective in degrading both structures in the stomach. They have also solved and established the three-dimensional structure and chemical mechanism of action of naproxen. Features such as its thermal stability, its pH profile, and its latency period, among others. 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 can be administered orally, similar to lactase tablets taken by patients. lactose intolerant”Scientists tell.


Such a treatment must have a molecule that is capable of breaking down toxic peptides and be harmless to intestine; It must be efficient enough to degrade toxic peptides in appropriate amounts in appropriate amounts; And it must be active before it can move to the gut, the researchers say.

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“The studies we conducted have allowed us to verify that naproxen has great potential to be developed as a drug, as it is comparable to other candidate proteolytic enzymes currently under study in extreme conditions of stomach digestion. is more active in Efficient glutenase requires prioritization», CSIC researcher F. Javier Gomis-Ruth explains.

“We are now going to move on to more specific tests to verify this capability before moving on to clinical trials and working with mutant molecules that may be even more efficient.”

33-mer peptide It is one of the main causes of celiac disease, as it results from the degradation of prolamin in wheat, one of the most widespread grains on the market. Wheat gluten is easily found in countless food, pharmaceutical and cosmetic products.

“The 33-mer is the most toxic peptide produced from gliadin and it remains to be seen whether its elimination will be sufficient to eliminate the manifestations and pathogenic responses of celiac disease,” says Francisco José Pérez Cano, a researcher at the university. Barcelona.

Nation World News Desk
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