Article ID Journal Published Year Pages File Type
1375415 Bioorganic & Medicinal Chemistry Letters 2008 4 Pages PDF
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 (KI∗=4.4nM) and had potent antibacterial activity against Gram-positive bacterium Bacillus subtilis (MIC = 2–4 μg/mL).

Graphical abstractMacrocyclic 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 (KI∗=4.4nM) and had potent antibacterial activity against Gram-positive bacterium Bacillus subtilis (MIC = 2–4 μg/mL).Figure optionsDownload full-size imageDownload as PowerPoint slide

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Physical Sciences and Engineering Chemistry Organic Chemistry
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