title: Design and synthesis of macrocyclic peptidyl hydroxamates as peptide deformylase inhibitors.
abstract: Macrocyclic peptidyl hydroxamates were designed, synthesized, and evaluated as peptide deformylase (PDF) inhibitors. The most potent compound exhibited tight, slow-binding inhibition of Escherichia coli PDF (K(I)(*)=4.4 nM) and had potent antibacterial activity against Gram-positive bacterium Bacillus subtilis (MIC=2-4 microg/mL).
authors: Department of Chemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH 43210, USA.
authors: Gang
authors: G
authors: Shen
authors: Jinge
authors: J
authors: Zhu
authors: Anthony M
authors: AM
authors: Simpson
authors: Dehua
authors: D
authors: Pei
mesh_terms: D000581:Amidohydrolases / Q000037:antagonists & inhibitors* / Q000737:chemistry; D000900:Anti-Bacterial Agents / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D001412:Bacillus subtilis / Q000187:drug effects*; D001667:Binding, Competitive / Q000187:drug effects; D002208:Caproates / Q000737:chemistry; D015195:Drug Design; D006877:Hydroxamic Acids / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D015394:Molecular Structure; D010456:Peptides, Cyclic / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D013329:Structure-Activity Relationship
chemical_list: D000900:Anti-Bacterial Agents; D002208:Caproates; D006877:Hydroxamic Acids; D010456:Peptides, Cyclic; D000581:Amidohydrolases; C084507:peptide deformylase