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A group led by Shoichet, now associate professor of pharmaceutical chemistry at the University of California, San Francisco, backs up that finding with a new study of aggregation-induced inhibition [J. Med. Chem., published online Aug. 22, http://dx.doi.org/10.1021/jm030266r]. The researchers determined a molecular mechanism by which aggregates can reversibly sequester an enzyme, resulting in apparent inhibition. And they confirmed that aggregation-induced activity is indeed attenuated by disrupting the aggregates using detergent.
"If this result is generally applicable in enzyme-screening assays," Shoichet says, "one might imagine a simple solution to a good proportion of aggregation-induced inhibition in screening--addition of small amounts of detergents to screening assays. Whereas showing that this is the case must await further experiment, these papers give some reason for optimism."
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