Title of article
Peptide deformylase inhibitors of Mycobacterium tuberculosis: Synthesis, structural investigations, and biological results
Author/Authors
Arkadius Pichota، نويسنده , , Jeyaraj Duraiswamy، نويسنده , , Zheng Yin، نويسنده , , Thomas H. Keller، نويسنده , , Jenefer Alam، نويسنده , , Sarah Liung، نويسنده , , Gladys Lee، نويسنده , , Mei - Ding Kao، نويسنده , , Gang Wang، نويسنده , , Wai-Ling Chan، نويسنده , , Mark Schreiber، نويسنده , , Ida Ma، نويسنده , , David Beer، نويسنده , , Xinyi Ngew، نويسنده , , Kakoli Mukherjee، نويسنده , , Mahesh Nanjundappa، نويسنده , , Jeanette W.P. Teo، نويسنده , , Pamela Thayalan، نويسنده , , Amelia Yap، نويسنده , , Thomas Dick، نويسنده , , et al.، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2008
Pages
5
From page
6568
To page
6572
Abstract
Bacterial peptide deformylase (PDF) belongs to a subfamily of metalloproteases catalyzing the removal of the N-terminal formyl group from newly synthesized proteins. We report the synthesis and biological activity of highly potent inhibitors of Mycobacterium tuberculosis (Mtb) PDF enzyme as well as the first X-ray crystal structure of Mtb PDF. Structure–activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency. Activities against single and multi-drug-resistant Mtb strains are also reported.
Keywords
Mycobacterium tuberculosis , x-ray , SAR , PDF , Antibacterial
Journal title
Bioorganic & Medicinal Chemistry Letters
Serial Year
2008
Journal title
Bioorganic & Medicinal Chemistry Letters
Record number
800283
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