Disease relevance of 235784-88-0

• To elucidate the interactions that contribute to the binding affinity of these inhibitors, we determined the crystal structures of BB-3497 and actinonin bound to Escherichia coli PDF at resolutions of 2.1 and 1.75 A, respectively [1].
• All PDF inhibitors were less active against Haemophilus influenzae; BB-3497 was the most active agent (MIC(90), 2 microg/ml) [2].
• The two-step inhibition model detailed herein for the inhibition of Staphylococcus aureus PDF by actinonin and BB-3497 is consistent with a recent report on the time-dependent inhibition of Escherichia coli PDF by a macrocyclic peptidomimetic inhibitor [Ngugen, K. T., et al. (2004) Bioorg. Chem. 32, 178-191] [3].
• BB-3497, a peptide deformylase inhibitor, is active against Mycobacterium tuberculosis [4].

High impact information on 235784-88-0

• Antibiotic activity and characterization of BB-3497, a novel peptide deformylase inhibitor [1].
• 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 [5].
• Structure-activity relationships of the peptide deformylase inhibitor BB-3497: modification of the methylene spacer and the P1' side chain [6].
• A series of analogues of the potent peptide deformylase (PDF) inhibitor BB-3497 containing alternative metal binding groups was synthesised [7].

Biological context of 235784-88-0

• Structure-activity relationships of the peptide deformylase inhibitor BB-3497: modification of the metal binding group [7].

Gene context of 235784-88-0

• In addition, we demonstrate that BB-3497 is also a time-dependent inhibitor of PDF with an extremely slow off-rate [3].

References