Peptide deformylase inhibitors with activity against respiratory tract pathogens

Autor:	Richard S. Todd, Mark Whittaker, Wayne Thomas, John M. Clements, Sheila Doel, Helen Smith, Daniel Christopher Brookings, Alison J. Thompson, Gilles Pain, Paul Beckett, Stephen P. East, Kenneth Keavey
Rok vydání:	2004
Předmět:	Clinical Biochemistry Pharmaceutical Science Microbial Sensitivity Tests Biochemistry Amidohydrolases Microbiology chemistry.chemical_compound Peptide deformylase Anti-Infective Agents Drug Discovery medicine Peptide bond Enzyme Inhibitors Respiratory Tract Infections Molecular Biology Antibacterial agent Hydroxamic acid Respiratory tract infections biology Organic Chemistry Biological activity Haemophilus influenzae Streptococcus pneumoniae medicine.anatomical_structure chemistry Enzyme inhibitor biology.protein Molecular Medicine Moraxella catarrhalis Respiratory tract
Zdroj:	Bioorganic & Medicinal Chemistry Letters. 14:59-62
ISSN:	0960-894X
DOI:	10.1016/j.bmcl.2003.10.013
Popis:	A series of analogues of the peptide deformylase (PDF) inhibitor BB-3497 where the P3' amide bond was replaced with a ketone functionality is described. The in vitro antibacterial profiling of these compounds revealed that they demonstrate activity against pathogens associated with respiratory tract infections.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3124655adf092283e47a34533311a1e https://doi.org/10.1016/j.bmcl.2003.10.013 Zobrazit plný text záznamu Full Text from ScienceDirect