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

Article Details

Citation

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
DrugTargetPropertyMeasurementpHTemperature (°C)
Bb-3497Peptide deformylase, mitochondrialIC 50 (nM)7N/AN/ADetails