Lee, KS Seo, SH Lee, YH Kim, HD Son, MH Chung, BY Lee, JY Jin, CB Lee, YS 2024-01-21T04:42:56Z 2024-01-21T04:42:56Z 2021-09-03 2005-06-02 0960-894X https://pubs.kist.re.kr/handle/201004/136368 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 mu-calpain inhibition. Among synthesized, compound 2i was the most potent calpain inhibitor with an IC50 value of 0.24 +/- 0.11 mu M comparable to the activity of peptide aldehyde calpain inhibitor MDL 28,170. Furthermore, compound 2i showed higher selectivity for mu-calpain over two related cysteine proteases cathepsin B and cathepsin L, suggesting the chromone ring as a good scaffold for selective mu-calpain inhibitors. (c) 2005 Elsevier Ltd. All rights reserved. English PERGAMON-ELSEVIER SCIENCE LTD SPINAL-CORD PEPTIDYL EXPLORATION Synthesis and biological evaluation of chrohlone carboxamides as calpain inhibitors Article 10.1016/j.bmcl.2005.03.095 1 BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, v.15, no.11, pp.2857 - 2860 BIOORGANIC & MEDICINAL CHEMISTRY LETTERS 15 11 2857 2860 scie scopus 000229665600032 2-s2.0-19544380408 Chemistry, Medicinal Chemistry, Organic Pharmacology & Pharmacy Chemistry Article SPINAL-CORD PEPTIDYL EXPLORATION calpain inhibitor chromone ischemia stroke