537711-86-7Relevant academic research and scientific papers
Structure-activity relationships of the peptide deformylase inhibitor BB-3497: Modification of the metal binding group
Smith, Helen K.,Beckett,Clements, John M.,Doel, Sheila,East, Stephen P.,Launchbury, Steven B.,Pratt, Lisa M.,Spavold, Zo? M.,Thomas, Wayne,Todd, Richard S.,Whittaker, Mark
, p. 3595 - 3599 (2002)
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.
