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Nuclear magnetic resonance aids in drug design
Date:5/19/2010

ally understand how we should make ligand molecules, candidate drug molecules, floppy or not floppy, in order to best interfere with the target protein. For example, we can test the idea that some residual 'floppiness' in a drug may help it co-adapt with a protein target site that 'morphs' over time, on account of drug-resistant mutations. We can also study how drug 'floppiness' can affect its ability to cross biological membranes and reach its protein target."

Peng, who worked as a biophysicist at a pharmaceutical company for 10 years before he came to Notre Dame, said the study of flexibility-activity relationships (FARs) adds another dimension to the longstanding structure-activity relationships (SARs) that scientists have studied. Addressing the dynamism of both the target molecule and the drug molecule can provide important resources for drug designers.

"If you could know, atom by atom, which parts have to move and which do not have to move to bind to a target protein, that's information a chemist can use," he says. "They can change the ligand as chemists do, repeat the activity assay, and see if it has improved."


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Contact: Jeffrey Peng
jpeng@nd.edu
574-631-2983
University of Notre Dame
Source:Eurekalert

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