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Scripps Florida scientists awarded $1.5M to fight major water and food parasites
Date:10/28/2008

akes these proteases attractive as therapeutic targets is that they are found in a number of different parasites, and that synthetic inhibitor libraries have already been developed against this enzyme family.

As a result, a wealth of inhibitor leads already exist, many of which have been subject to extensive pharmacokinetic and safety studies; for example cysteine protease inhibitors have already demonstrated potent anti-trypanosomal effects.

"This family of enzymes is well known biochemically and structurally," Roush said, "and we understand the relationship between structure and function that involves active site specificity. Our laboratory has used this information to help design new inhibitors that attack targets critical to invasive Entamoeba histolytica."

The new inhibitor designed by Roush's laboratory attacks the EhCP1 (Entamoeba histolytica cysteine proteinase), which is believed to be a virulence factor of this parasite.

"We have designed a compound that has very good properties as an inhibitor of this particular protease," Roush said. "When you kill this enzyme, you kill the parasite's ability to infect human tissue. In animal models, this molecule behaves beautifully in that capacity. Unfortunately, it's not an orally bioavailable compound, so right now we're working to optimize it to make it orally available."


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Contact: Keith McKeown
kmckeown@scripps.edu
858-784-8134
Scripps Research Institute
Source:Eurekalert

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