Bioorg Med Chem Lett. 2002 Dec 16;12(24):3595-9.

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

Smith HK, Beckett RP, Clements JM, Doel S, East SP, Launchbury SB, Pratt LM, Spavold ZM, Thomas W, Todd RS, Whittaker M.

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British Biotech Pharmaceuticals Limited, Watlington Road, Oxford OX4 6LY, UK.

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.

PMID:: 12443784; [PubMed - indexed for MEDLINE]

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