Significance of hydrogen bonding at the S 1′ subsite of calpain I

IO Donkor, X Zheng, J Han, C Lacy, DD Miller

Index: Donkor, Isaac O.; Zheng, Xiaozhang; Han, Jie; Lacy, Calvin; Miller, Duane D. Bioorganic and Medicinal Chemistry Letters, 2001 , vol. 11, # 13 p. 1753 - 1755

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Citation Number: 26

Abstract

α-Ketohydroxamates were synthesized as bioisosteres of α-ketoamides. The α- ketohydroxamates were generally more potent than the corresponding α-ketoamides. The potency of the compounds suggests that hydrogen bonding and steric bulk of substituents on the nitrogen atom of the ketoamide moiety influence calpain inhibition.

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