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Team:UC Davis/Treatments
From 2009.igem.org
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=Current Treatments= | =Current Treatments= | ||
| - | Currently, no cure | + | Currently, there is no cure for this genetic condition. Prevention of the symptoms associated with celiac disease is accomplished through adopting a gluten free diet (14, 12, 11). Gluten is present in most everyday diets; it is very hard to have a gluten-free diet. |
| - | "Oral supplementation with prolyl oligopeptidases has therefore been proposed as a potential therapeutic approach."(8) | + | "Oral supplementation with prolyl oligopeptidases has therefore been proposed as a potential therapeutic approach."(8) However, enzymes studied earlier were not able to degrade gluten (inside stomach before it reaches small intestine because they were "irreversibly inactivated by pepsin and acidic pH, both present in the stomach."(8) |
| - | + | Over the past years, researchers have discovered an enzyme from the bacterium ''Aspergillus niger''. A newly identified prolyl endoprotease, was observed to "work optimally at 4-5 pH and remains stable at 2 pH".(8) This enzyme has the possibility of leading us to an alternative treatment for this condition. (8) Studies have shown that prolyl-endoprotease is able to "degrade gluten in vitro and under conditions similar to the ones present in the gastrointestinal tract." (8) ; but due to licensing restrictions we have opted not to work with this protein. | |
| - | + | In 2007, a study suggested an alternative approach by combining a glutamine-specific endoprotease (EP-B2 from barley) and a prolyl endopeptidase (SC PEP from ''Sphingomonas capsulata''); with gastric activity and complementary substrate specificity there is a possibility of increasing the safe threshold of ingested gluten (12). An advantage of this “combination product is that both enzymes are active and stable in stomach and can therefore be administered as lyophilized powders or simple capsules or tablets” (12). | |
| - | ''Note: | + | ''Note: This study was first “evaluated via in vitro digestion of whole-wheat bread and then confirmed by in vivo studies in rats (12), unlike other earlier studies which were performed on synthetic gluten oligopeptides, recombinant gliadin proteins, or uncooked gluten” (12).'' |
Revision as of 22:03, 22 September 2009
Current Treatments
Currently, there is no cure for this genetic condition. Prevention of the symptoms associated with celiac disease is accomplished through adopting a gluten free diet (14, 12, 11). Gluten is present in most everyday diets; it is very hard to have a gluten-free diet.
"Oral supplementation with prolyl oligopeptidases has therefore been proposed as a potential therapeutic approach."(8) However, enzymes studied earlier were not able to degrade gluten (inside stomach before it reaches small intestine because they were "irreversibly inactivated by pepsin and acidic pH, both present in the stomach."(8)
Over the past years, researchers have discovered an enzyme from the bacterium Aspergillus niger. A newly identified prolyl endoprotease, was observed to "work optimally at 4-5 pH and remains stable at 2 pH".(8) This enzyme has the possibility of leading us to an alternative treatment for this condition. (8) Studies have shown that prolyl-endoprotease is able to "degrade gluten in vitro and under conditions similar to the ones present in the gastrointestinal tract." (8) ; but due to licensing restrictions we have opted not to work with this protein.
In 2007, a study suggested an alternative approach by combining a glutamine-specific endoprotease (EP-B2 from barley) and a prolyl endopeptidase (SC PEP from Sphingomonas capsulata); with gastric activity and complementary substrate specificity there is a possibility of increasing the safe threshold of ingested gluten (12). An advantage of this “combination product is that both enzymes are active and stable in stomach and can therefore be administered as lyophilized powders or simple capsules or tablets” (12).
Note: This study was first “evaluated via in vitro digestion of whole-wheat bread and then confirmed by in vivo studies in rats (12), unlike other earlier studies which were performed on synthetic gluten oligopeptides, recombinant gliadin proteins, or uncooked gluten” (12).
