Macrocyclic inhibitors for peptide deformylase: a structure-activity relationship study of the ring size

X Hu, KT Nguyen, VC Jiang, D Lofland…

Index: Hu, Xubo; Nguyen, Kiet T.; Jiang, Vernon C.; Lofland, Denene; Moser, Heinz E.; Pei, Dehua Journal of Medicinal Chemistry, 2004 , vol. 47, # 20 p. 4941 - 4949

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Citation Number: 53

Abstract

Peptide deformylase (PDF) catalyzes the removal of the N-terminal formyl group from newly synthesized polypeptides in eubacteria. Its essential role in bacterial cells but not in mammalian cells makes it an attractive target for antibacterial drug design. We have previously reported an N-formylhydroxylamine-based, metal-chelating macrocyclic PDF inhibitor, in which the P1'and P3'side chains are covalently joined. In this work, we have ...