title: Significance of hydrogen bonding at the S(1)' subsite of calpain I.
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.
authors: Department of Pharmaceutical Sciences, The University of Tennessee, Johnson Bldg. Room 327E, 847Monroe Avenue, TN 38163, Memphis, USA. idonkor@utmem.edu
authors: I O
authors: IO
authors: Donkor
authors: X
authors: X
authors: Zheng
authors: J
authors: J
authors: Han
authors: C
authors: C
authors: Lacy
authors: D D
authors: DD
authors: Miller
mesh_terms: D002154:Calpain / Q000737:chemistry*; D006860:Hydrogen Bonding
chemical_list: D002154:Calpain