Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1365197 | Bioorganic & Medicinal Chemistry Letters | 2008 | 4 Pages |
Abstract
A family of aryl-substituted maleimides was prepared and studied for their activity against calmodulin-dependant kinase. Inhibitory activities against the enzyme ranged from 34 nM to >20 μM and were dependant upon both the nature of the aryl group and the tether joining the basic amine to the indolyl maleimide core. Key interactions with the kinase ATP site and hinge region, predicted by homology modeling, were confirmed.
Graphical abstractAryl-substituted maleimides were prepared and studied for their activity against CaMKIIδ. Inhibitory activities ranged from 34 nM to >20 μM. Key predicted interactions with the kinase ATP site and hinge region were confirmed.Figure optionsDownload full-size imageDownload as PowerPoint slide
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Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Daniel E. Levy, Dan-Xiong Wang, Qing Lu, Zheng Chen, John Perumattam, Yong-jin Xu, Jeffrey Higaki, Hanmin Dong, Albert Liclican, Maureen Laney, Babu Mavunkel, Sundeep Dugar,