Structure-activity relationships of the peptide deformylase inhibitor BB-3497: modification of the metal binding group.
Article Details
- CitationCopy to clipboard
Smith HK, Beckett RP, Clements JM, Doel S, East SP, Launchbury SB, Pratt LM, Spavold ZM, Thomas W, Todd RS, Whittaker M
Structure-activity relationships of the peptide deformylase inhibitor BB-3497: modification of the metal binding group.
Bioorg Med Chem Lett. 2002 Dec 16;12(24):3595-9.
- PubMed ID
- 12443784 [ View in PubMed]
- Abstract
A series of analogues of the potent peptide deformylase (PDF) inhibitor BB-3497 containing alternative metal binding groups was synthesised. Enzyme inhibition and antibacterial activity data for these compounds revealed that the bidentate hydroxamic acid and N-formyl hydroxylamine structural motifs represent the optimum chelating groups on the pseudopeptidic BB-3497 backbone.
DrugBank Data that Cites this Article
- Binding Properties
Drug Target Property Measurement pH Temperature (°C) Bb-3497 Peptide deformylase, mitochondrial IC 50 (nM) 7 N/A N/A Details