Chalcones as Novel Non-peptidic μ-Calpain Inhibitors

In order to extend the scaffold of non-peptidic calpain inhibitor, we have designed and synthesized 14 chalcone derivatives categorized into two groups based on their structures. Compounds 7 (IC_50 = 16.67 ± 0.42 μM) and 8 (IC_50 = 16.92 ± 0.14 μM) in group A were most selective μ-calpain inhibitor...

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Bibliographic Details
Published in:Bulletin of the Korean Chemical Society 2011, 32(9), , pp.3459-3464
Main Authors: Lee, Eun-Young, Jang, In-Hye, Shin, Min-Jung, Cho, Hee-Ju, Kim, Jung-Sook, Eom, Ji-Eun, Kwon, Young-Joo
Format: Article
Language:English
Subjects:
화학
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Summary:In order to extend the scaffold of non-peptidic calpain inhibitor, we have designed and synthesized 14 chalcone derivatives categorized into two groups based on their structures. Compounds 7 (IC_50 = 16.67 ± 0.42 μM) and 8 (IC_50 = 16.92 ± 0.14 μM) in group A were most selective μ-calpain inhibitor over cathepsins B and L. On the other hand, compound 14 possessing furan ring exhibited inhibitory activities for μ-calpain (IC_50 = 15.39 ± 1.34μM) as well as cathepsin B (IC_50 = 20.59 ± 1.35 μM). The results discovered implicated that chalcone analogues possessing proper size and functional groups can be a potential lead core for selective non-peptidic μ-calpain inhibitor. Furthermore, dual inhibitors for μ-calpain and cathepsin B can also be developed from chalcones by elaborate structure manipulation. KCI Citation Count: 8
ISSN:0253-2964
1229-5949
DOI:10.5012/bkcs.2011.32.9.3459