Bioorganic & medicinal chemistry letters

Peptidyl hydroxamic acids as methionine aminopeptidase inhibitors

X Hu, J Zhu, S Srivathsan, D Pei

Index: Hu, Xubo; Zhu, Jinge; Srivathsan, Sumant; Pei, Dehua Bioorganic and Medicinal Chemistry Letters, 2004 , vol. 14, # 1 p. 77 - 79

Full Text: HTML

Citation Number: 33

Abstract

A new class of methionine aminopeptidase (MetAP) inhibitors, which contain an internal hydroxamate (N-acyl-N-alkylhydroxylamine) core as the metal-chelating group, has been designed, synthesized, and tested. The compounds exhibited reversible, competitive inhibition against Escherichia coli MetAP as well as human MetAP-1 and MetAP-2. The most potent inhibitor had a Ki value of 2.5 μM and> 20-fold selectivity toward E. coli MAP.

Related Articles:

Enzymatic peptidyl. alpha.-amidation proceeds through formation of an. alpha.-hydroxyglycine intermediate

[Young, Stanley D.; Tamburini, Paul P. Journal of the American Chemical Society, 1989 , vol. 111, # 5 p. 1933 - 1934]

Synthesis and aldose reductase inhibitory activity of N-(arylsulfonyl)-and N-(aroyl)-N-(arylmethyloxy) glycines

[Balsamo, A.; Belfiore, M. S.; Macchia, M.; Martini, C.; Nencetti, S.; et al. European Journal of Medicinal Chemistry, 1994 , vol. 29, # 10 p. 787 - 794]

More Articles...