Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1376006 | Bioorganic & Medicinal Chemistry Letters | 2005 | 4 Pages |
Abstract
Excessive calpain activations contribute to serious cellular damage and have been found in many pathological conditions. Novel chromone carboxamides derived from ketoamides were prepared and evaluated for μ-calpain inhibition. Among synthesized, compound 2i was the most potent calpain inhibitor with an IC50 value of 0.24 ± 0.11 μM comparable to the activity of peptide aldehyde calpain inhibitor MDL 28,170. Furthermore, compound 2i showed higher selectivity for μ-calpain over two related cysteine proteases cathepsin B and cathepsin L, suggesting the chromone ring as a good scaffold for selective μ-calpain inhibitors.
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Related Topics
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Chemistry
Organic Chemistry
Authors
Kwang Seob Lee, Seon Hee Seo, Yong Ha Lee, Ha Dong Kim, Moon Ho Son, Bong Young Chung, Jae Yeol Lee, Changbae Jin, Yong Sup Lee,