Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1375415 | Bioorganic & Medicinal Chemistry Letters | 2008 | 4 Pages |
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
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Gang Shen, Jinge Zhu, Anthony M. Simpson, Dehua Pei,