Significance of hydrogen bonding at the S(1)' subsite of calpain I

I O Donkor; X Zheng; J Han; C Lacy; D D Miller

doi:10.1016/s0960-894x(01)00301-8

Significance of hydrogen bonding at the S(1)' subsite of calpain I

Bioorg Med Chem Lett. 2001 Jul 9;11(13):1753-5. doi: 10.1016/s0960-894x(01)00301-8.

Authors

I O Donkor¹, X Zheng, J Han, C Lacy, D D Miller

Affiliation

¹ Department of Pharmaceutical Sciences, The University of Tennessee, Johnson Bldg. Room 327E, 847Monroe Avenue, TN 38163, Memphis, USA. idonkor@utmem.edu

PMID: 11425553
DOI: 10.1016/s0960-894x(01)00301-8

Abstract

alpha-Ketohydroxamates were synthesized as bioisosteres of alpha-ketoamides. The alpha-ketohydroxamates were generally more potent than the corresponding alpha-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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Calpain / chemistry*
Hydrogen Bonding*

Substances

Calpain

Grants and funding

5 K14 HL03536/HL/NHLBI NIH HHS/United States