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"It relies on using smaller, "chaperone" molecules to keep proteins on the right track toward proper folding, but their biochemical mechanism is not well understood."
"The interactions we looked at are exactly the things occurring in the clinical trial right now. The same concept is now being applied to other protein-folding diseases such as Parkinson's and Alzheimer's diseases. Many medical researchers are trying to keep proteins from misfolding by using small chaperone molecules. Our studies have definitely advanced the understanding of how to do that."
"Tight is better, because you can use less of the drug for treatment. We now can explain DGJ's high potency, its tight binding, down to individual atoms."
"It was surprising to find these two small molecules that look very much the same have very different affinities for this enzyme, and we now understand why. The iminosugar DGJ has high potency due to a single ionic interaction with α-GAL. Overall, our studies show that this small molecule keeps the enzyme from unfolding, or when it unfolds, the process happens more slowly, all of which you need in treating disease."
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12 Dec. 2013. <http://www.medicalnewstoday.com/articles/239979>
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